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Volumn 28, Issue 2, 1997, Pages 241-260

Structural trees for protein superfamilies

Author keywords

Protein modeling; Protein structure comparison; Stepwise folding; Structural motif; Structural similarity

Indexed keywords

PROTEIN;

EID: 0030910802     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<241::AID-PROT12>3.0.CO;2-I     Document Type: Article
Times cited : (83)

References (254)
  • 1
    • 0016162558 scopus 로고
    • Algorithm for prediction of α-helical and β-structural regions in globular proteins
    • Lim, V.I. Algorithm for prediction of α-helical and β-structural regions in globular proteins. J. Mol. Biol. 88:873-894, 1974.
    • (1974) J. Mol. Biol. , vol.88 , pp. 873-894
    • Lim, V.I.1
  • 2
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P.Y., Fasman, G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47:45-148, 1978.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 3
    • 0020648054 scopus 로고
    • Theory of protein secondary structure and algorithm of its prediction
    • Ptitsyn, O.B., Finkelstein, A.V. Theory of protein secondary structure and algorithm of its prediction. Biopolymers 22:15-25, 1983.
    • (1983) Biopolymers , vol.22 , pp. 15-25
    • Ptitsyn, O.B.1    Finkelstein, A.V.2
  • 5
    • 0000920828 scopus 로고
    • The packing of α helices: Simple coiled-coils
    • Crick, F.H.C. The packing of α helices: Simple coiled-coils. Acta Crystallogr. 6:689-697, 1953.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 6
    • 0343063933 scopus 로고
    • Structure of proteins: Packing of α helices and pleated sheets
    • Chothia, C., Levitt, M., Richardson, D. Structure of proteins: Packing of α helices and pleated sheets. Proc. Natl. Acad. Sci. U.S.A. 74:4130-4134, 1977.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 4130-4134
    • Chothia, C.1    Levitt, M.2    Richardson, D.3
  • 7
    • 0017780710 scopus 로고
    • Stereochemistry of packing of α helices and β-structure in a compact globule
    • Efimov, A.V. Stereochemistry of packing of α helices and β-structure in a compact globule. Dokl. Akad. Nauk S.S.S.R. 235:699-702, 1977.
    • (1977) Dokl. Akad. Nauk S.S.S.R. , vol.235 , pp. 699-702
    • Efimov, A.V.1
  • 8
    • 0017876485 scopus 로고
    • Packing of α helices: Geometrical constraints and contact areas
    • Richmond, T.J., Richards, F.M. Packing of α helices: Geometrical constraints and contact areas. J. Mol. Biol. 119:537-555, 1978.
    • (1978) J. Mol. Biol. , vol.119 , pp. 537-555
    • Richmond, T.J.1    Richards, F.M.2
  • 9
    • 0018792414 scopus 로고
    • Packing of α helices in globular proteins. Layer-structure of globin hydrophobic cores
    • Efimov, A.V. Packing of α helices in globular proteins. Layer-structure of globin hydrophobic cores. J. Mol. Biol. 134:23-40, 1979.
    • (1979) J. Mol. Biol. , vol.134 , pp. 23-40
    • Efimov, A.V.1
  • 11
    • 0020485895 scopus 로고
    • Orthogonal packing of β-pleated sheets in proteins
    • Chothia, C., Janin, J. Orthogonal packing of β-pleated sheets in proteins. Biochemistry 21:3955-3965, 1982.
    • (1982) Biochemistry , vol.21 , pp. 3955-3965
    • Chothia, C.1    Janin, J.2
  • 12
    • 0024279564 scopus 로고
    • General architecture of the α-helical globule
    • Murzin, A.G., Finkelstein, A.V. General architecture of the α-helical globule. J. Mol. Biol. 204:749-769, 1988.
    • (1988) J. Mol. Biol. , vol.204 , pp. 749-769
    • Murzin, A.G.1    Finkelstein, A.V.2
  • 13
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao, S.T., Rossmann, M.G. Comparison of super-secondary structures in proteins. J. Mol. Biol. 76:241-256, 1973.
    • (1973) J. Mol. Biol. , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 14
    • 0017073680 scopus 로고
    • On the conformation of proteins: The handedness of the β strand-α helix-β strand unit
    • Sternberg, M.J.E., Thornton, J. M. On the conformation of proteins: The handedness of the β strand-α helix-β strand unit. J. Mol. Biol. 105:367-382, 1976.
    • (1976) J. Mol. Biol. , vol.105 , pp. 367-382
    • Sternberg, M.J.E.1    Thornton, J.M.2
  • 15
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • Levitt, M., Chothia, C. Structural patterns in globular proteins. Nature 261:552-558, 1976.
    • (1976) Nature , vol.261 , pp. 552-558
    • Levitt, M.1    Chothia, C.2
  • 16
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34:167-339, 1981.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 17
    • 0020360290 scopus 로고
    • Super-secondary structure of β proteins
    • Efimov, A.V. Super-secondary structure of β proteins. Mol. Biol. 16:799-806, 1982.
    • (1982) Mol. Biol. , vol.16 , pp. 799-806
    • Efimov, A.V.1
  • 18
    • 0021769164 scopus 로고
    • A novel super-secondary structure of proteins and the relation between the structure and the amino acid sequence
    • Efimov, A.V. A novel super-secondary structure of proteins and the relation between the structure and the amino acid sequence. FEBS Lett. 166:33-38, 1984.
    • (1984) FEBS Lett. , vol.166 , pp. 33-38
    • Efimov, A.V.1
  • 19
    • 0024722728 scopus 로고
    • Topological distribution of four-α helix bundles
    • Presnell, S.R., Cohen, F.E. Topological distribution of four-α helix bundles. Proc. Natl. Acad. Sci. U.S.A. 86:6592-6596, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6592-6596
    • Presnell, S.R.1    Cohen, F.E.2
  • 20
    • 0025803604 scopus 로고
    • Structure of coiled β-β hairpins and β-β corners
    • Efimov, A.V. Structure of coiled β-β hairpins and β-β corners. FEBS Lett. 284:288-292, 1991.
    • (1991) FEBS Lett. , vol.284 , pp. 288-292
    • Efimov, A.V.1
  • 21
    • 0026602058 scopus 로고
    • A novel super-secondary structure of β proteins: A triple-strand corner
    • Efimov, A.V. A novel super-secondary structure of β proteins: A triple-strand corner. FEBS Lett. 298:261-265, 1992.
    • (1992) FEBS Lett. , vol.298 , pp. 261-265
    • Efimov, A.V.1
  • 22
    • 0027501615 scopus 로고
    • Super-secondary structures involving triple-strand β sheets
    • Efimov, A.V. Super-secondary structures involving triple-strand β sheets. FEBS Lett. 334:253-256, 1993.
    • (1993) FEBS Lett. , vol.334 , pp. 253-256
    • Efimov, A.V.1
  • 23
    • 0027918137 scopus 로고
    • Alpha plus beta folds revisited: Some favoured motifs
    • Orengo, C.A., Thornton, J.M. Alpha plus beta folds revisited: Some favoured motifs. Structure 1:105-120, 1993.
    • (1993) Structure , vol.1 , pp. 105-120
    • Orengo, C.A.1    Thornton, J.M.2
  • 24
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A.G. OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences. EMBO J. 12:861-867, 1993.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 25
    • 0027428284 scopus 로고
    • Standard structures in proteins
    • Efimov, A.V. Standard structures in proteins. Prog. Biophys. Mol. Biol. 60:201-239, 1993.
    • (1993) Prog. Biophys. Mol. Biol. , vol.60 , pp. 201-239
    • Efimov, A.V.1
  • 26
    • 0028774532 scopus 로고
    • Favoured structural motifs in globular proteins
    • Efimov, A.V. Favoured structural motifs in globular proteins. Structure 2:999-1002, 1994.
    • (1994) Structure , vol.2 , pp. 999-1002
    • Efimov, A.V.1
  • 27
    • 0027949057 scopus 로고
    • Common structural motifs in small proteins and domains
    • Efimov, A.V. Common structural motifs in small proteins and domains. FEBS Lett. 355:213-219, 1994.
    • (1994) FEBS Lett. , vol.355 , pp. 213-219
    • Efimov, A.V.1
  • 28
    • 0018474290 scopus 로고
    • Principal folding pathway and topology of all-β proteins
    • Ptitsyn, O.B., Finkelstein, A.V., Falk (Bendzko), P. Principal folding pathway and topology of all-β proteins. FEBS Lett. 101:1-5, 1979.
    • (1979) FEBS Lett. , vol.101 , pp. 1-5
    • Ptitsyn, O.B.1    Finkelstein, A.V.2    Falk, P.3
  • 29
    • 0019053499 scopus 로고
    • Similarities of protein topologies: Evolutionary divergence, functional convergence or principles of folding?
    • Ptitsyn, O.B., Finkelstein, A.V. Similarities of protein topologies: Evolutionary divergence, functional convergence or principles of folding? Q. Rev. Biophys. 13:339-386, 1980.
    • (1980) Q. Rev. Biophys. , vol.13 , pp. 339-386
    • Ptitsyn, O.B.1    Finkelstein, A.V.2
  • 30
    • 0001475624 scopus 로고
    • Protein folding: General physical model
    • Ptitsyn, O.B. Protein folding: General physical model. FEBS Lett. 131:197-202, 1981.
    • (1981) FEBS Lett. , vol.131 , pp. 197-202
    • Ptitsyn, O.B.1
  • 31
    • 0016671420 scopus 로고
    • A model of myoglobin self-organization
    • Ptitsyn, O.B., Rashin, A.A. A model of myoglobin self-organization. Biophys. Chem. 3:1-20, 1975.
    • (1975) Biophys. Chem. , vol.3 , pp. 1-20
    • Ptitsyn, O.B.1    Rashin, A.A.2
  • 32
    • 0028953472 scopus 로고
    • Structural similarity between two-layer α/β and β proteins
    • Efimov, A.V. Structural similarity between two-layer α/β and β proteins. J. Mol. Biol. 245:402-415, 1995.
    • (1995) J. Mol. Biol. , vol.245 , pp. 402-415
    • Efimov, A.V.1
  • 33
    • 0017904746 scopus 로고
    • A stereochemical theory of globular protein tertiary structure. I. Highly helical intermediate structures
    • Lim, V.I., Mazanov, A.L., Efimov, A.V. A stereochemical theory of globular protein tertiary structure. I. Highly helical intermediate structures. Mol. Biol. 12:206-213. 1978.
    • (1978) Mol. Biol. , vol.12 , pp. 206-213
    • Lim, V.I.1    Mazanov, A.L.2    Efimov, A.V.3
  • 34
    • 0017387723 scopus 로고
    • β-Sheet topology and the relatedness of proteins
    • Richardson, J.S. β-Sheet topology and the relatedness of proteins. Nature 268:495-500, 1977.
    • (1977) Nature , vol.268 , pp. 495-500
    • Richardson, J.S.1
  • 35
    • 0029565831 scopus 로고
    • Crystal structural of SIV matrix antigen and implications for virus assembly
    • Rao, Z., Belyaev, A.S., Fry, E., Roy, P., Jones, I.M., Stuart, D.I. Crystal structural of SIV matrix antigen and implications for virus assembly. Nature 378:743-747, 1995.
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jones, I.M.5    Stuart, D.I.6
  • 36
    • 0029927855 scopus 로고    scopus 로고
    • The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0Å resolution
    • Kurihara, H., Nonaka, T., Mitsui, Y., Ohgi, K., Irie, M., Nakamura, K.T. The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0Å resolution. J. Mol. Biol. 255:310-320, 1996.
    • (1996) J. Mol. Biol. , vol.255 , pp. 310-320
    • Kurihara, H.1    Nonaka, T.2    Mitsui, Y.3    Ohgi, K.4    Irie, M.5    Nakamura, K.T.6
  • 37
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U., Eklund, H. Structure of ribonucleotide reductase protein R1. Nature 370:533-539, 1994.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 38
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8Å resolution
    • Hart, P.J., Pfluger, H.D., Monzingo, A.F., Hollis, T., Robertus, J.D. The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8Å resolution. J. Mol. Biol. 248:402-413, 1995.
    • (1995) J. Mol. Biol. , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 40
    • 0019456340 scopus 로고
    • Structure of the cro repressor from bacteriophage λ and its interaction with DNA
    • Anderson, W.F., Ohlendorf, D.H., Takeda, Y., Matthews, B.W. Structure of the cro repressor from bacteriophage λ and its interaction with DNA. Nature 290:754-758, 1981.
    • (1981) Nature , vol.290 , pp. 754-758
    • Anderson, W.F.1    Ohlendorf, D.H.2    Takeda, Y.3    Matthews, B.W.4
  • 41
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J.T., Graziano, V., Lee, P.L., Sweet, R.M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature 362:219-223, 1993.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 42
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark, K.L., Halay, E.D., Lai, E., Burley, S.K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 364:412-420, 1993.
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 43
    • 0020490955 scopus 로고
    • Structure of catabolite gene activator protein at 2.9-Å resolution
    • McKay, D.B., Weber, I.T., Steitz, T.A. Structure of catabolite gene activator protein at 2.9-Å resolution. J. Biol. Chem. 257:9518-9524, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9518-9524
    • McKay, D.B.1    Weber, I.T.2    Steitz, T.A.3
  • 45
    • 0019977222 scopus 로고
    • The operator-binding domain of λ repressor: Structure and DNA recognition
    • Pabo, C.O., Lewis, M. The operator-binding domain of λ repressor: Structure and DNA recognition. Nature 298: 443-447, 1982.
    • (1982) Nature , vol.298 , pp. 443-447
    • Pabo, C.O.1    Lewis, M.2
  • 46
    • 0024961628 scopus 로고
    • Structure of the amino-terminal domain of phage 434 repressor at 2.0Å resolution
    • Mondragon, A., Subbiah, S., Almo, S.C., Drottar, M., Harrison, S.C. Structure of the amino-terminal domain of phage 434 repressor at 2.0Å resolution. J. Mol. Biol. 205:189-200, 1989.
    • (1989) J. Mol. Biol. , vol.205 , pp. 189-200
    • Mondragon, A.1    Subbiah, S.2    Almo, S.C.3    Drottar, M.4    Harrison, S.C.5
  • 47
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • Klemm, J.D., Rould, M.A., Aurora, R., Herr, W., Pabo, C.O. Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77:21-32, 1994.
    • (1994) Cell , vol.77 , pp. 21-32
    • Klemm, J.D.1    Rould, M.A.2    Aurora, R.3    Herr, W.4    Pabo, C.O.5
  • 48
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J.L., Bardwell, J.C.A., Kuriyan, J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365:464-468, 1993.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.A.2    Kuriyan, J.3
  • 49
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer, and ddCTP
    • Pelletier, H., Sawaya, M.R., Kumar, A., Wilson, S.H., Kraut, J. Structures of ternary complexes of rat DNA polymerase β, a DNA template-primer, and ddCTP. Science 264:1891-1898, 1994.
    • (1994) Science , vol.264 , pp. 1891-1898
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 50
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim, Y., Eom, S.H., Wang, J., Lee, D.-S., Suh, S.W., Steitz, T.A. Crystal structure of Thermus aquaticus DNA polymerase. Nature 376:612-616, 1995.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1    Eom, S.H.2    Wang, J.3    Lee, D.-S.4    Suh, S.W.5    Steitz, T.A.6
  • 51
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud, J-P., Rochel, N., Ruff, M., Vivat, V., Chambon, P., Gronemeyer, H., Moras, D. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378:681-689, 1995.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.-P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 53
    • 0020462668 scopus 로고
    • Structure of thermolysin refined at 1.6 Å resolution
    • Holmes, M.A., Matthews, B.W. Structure of thermolysin refined at 1.6 Å resolution. J. Mol. Biol. 160:623-639, 1982.
    • (1982) J. Mol. Biol. , vol.160 , pp. 623-639
    • Holmes, M.A.1    Matthews, B.W.2
  • 54
    • 0020483375 scopus 로고
    • Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution
    • Remington, S., Wiegand, G., Huber, R. Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 Å resolution. J. Mol. Biol. 158:111-152, 1982.
    • (1982) J. Mol. Biol. , vol.158 , pp. 111-152
    • Remington, S.1    Wiegand, G.2    Huber, R.3
  • 56
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution
    • Finzel, B.C., Poulos, T.L., Kraut, J. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution. J. Biol. Chem. 259:13027-13036, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 58
    • 0000539364 scopus 로고
    • Glucose-induced conformational change in yeast hexokinase
    • Bennet, W.S., Jr., Steitz, T.A. Glucose-induced conformational change in yeast hexokinase. Proc. Natl. Acad. Sci. USA 75:4848-4852, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4848-4852
    • Bennet Jr., W.S.1    Steitz, T.A.2
  • 59
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber, R., Romisch, J., Paques, E.-P. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 9:3867-3874, 1990.
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, J.2    Paques, E.-P.3
  • 60
    • 0027202271 scopus 로고
    • Crystal structure of hydrophobic protein from soybean: A member of a new cysteine-rich family
    • Baud, F., Pebay-Peyroula, E., Cohen-Addad, C., Odani, S., Lehmann, M.S. Crystal structure of hydrophobic protein from soybean: A member of a new cysteine-rich family. J. Mol. Biol. 231:877-887, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 877-887
    • Baud, F.1    Pebay-Peyroula, E.2    Cohen-Addad, C.3    Odani, S.4    Lehmann, M.S.5
  • 61
    • 0029643949 scopus 로고
    • High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings
    • Shin, D.H., Lee, J.Y., Hwang, K.Y., Kim, K.K., Suh, S.W. High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure 3:189-199, 1995.
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 63
    • 0028865333 scopus 로고
    • Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
    • Pedersen, L.C., Benning, M.M., Holden, H.M. Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry 34: 13305-13311, 1995.
    • (1995) Biochemistry , vol.34 , pp. 13305-13311
    • Pedersen, L.C.1    Benning, M.M.2    Holden, H.M.3
  • 65
    • 0017736964 scopus 로고
    • The structure of horse methaemoglobin at 2.0Å resolution
    • Ladner, R.C., Heidner, E.J., Perutz, M.F. The structure of horse methaemoglobin at 2.0Å resolution. J. Mol. Biol. 114:385-414, 1977.
    • (1977) J. Mol. Biol. , vol.114 , pp. 385-414
    • Ladner, R.C.1    Heidner, E.J.2    Perutz, M.F.3
  • 66
    • 0026581661 scopus 로고
    • Refined structure of the pore-forming domain of colicin a at 2.4 Å resolution
    • Parker, M.W., Postma, J.P.M., Pattus, F., Tucker, A.D., Tsernoglou, D. Refined structure of the pore-forming domain of colicin A at 2.4 Å resolution. J. Mol. Biol. 224:639-657, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 639-657
    • Parker, M.W.1    Postma, J.P.M.2    Pattus, F.3    Tucker, A.D.4    Tsernoglou, D.5
  • 70
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X.M., Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature 358:209-215, 1992.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 71
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger, R.H., Nockolds, C.E. Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem. 248:3313-3326, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 74
    • 0027404572 scopus 로고
    • The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Kalia, Y.N., Brocklehurst, S.M., Hipps, D.S., Appella, E., Sakaguchi, K., Perham, R.N. The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. J. Mol. Biol. 230:323-341, 1993.
    • (1993) J. Mol. Biol. , vol.230 , pp. 323-341
    • Kalia, Y.N.1    Brocklehurst, S.M.2    Hipps, D.S.3    Appella, E.4    Sakaguchi, K.5    Perham, R.N.6
  • 75
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake, C.C.F., Geisow, M.J., Oatley, S.J., Rérat, B., Rérat, C. Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å. J. Mol. Biol. 121:339-356, 1978.
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3    Rérat, B.4    Rérat, C.5
  • 76
    • 0026723625 scopus 로고
    • Crystal structure determination at 2.3-Å resolution of human transthyretin-3′,5′-dibromo-2′,4,4′,6-tetrahydroxyaurone complex
    • Cyszak, E., Cody, V., Luft, J.R. Crystal structure determination at 2.3-Å resolution of human transthyretin-3′,5′-dibromo-2′,4,4′,6-tetrahydroxyaurone complex. Proc. Natl. Acad. Sci. U.S.A. 89:6644-6648, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6644-6648
    • Cyszak, E.1    Cody, V.2    Luft, J.R.3
  • 77
    • 0026027728 scopus 로고
    • Structure of cyclodextrin glycosyl-transferase refined at 2.0 Å resolution
    • Klein, C., Schulz, G.E. Structure of cyclodextrin glycosyl-transferase refined at 2.0 Å resolution. J. Mol. Biol. 217:737-750, 1991.
    • (1991) J. Mol. Biol. , vol.217 , pp. 737-750
    • Klein, C.1    Schulz, G.E.2
  • 78
    • 0028067892 scopus 로고
    • Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution
    • Ohlendorf, D.H., Orville, A.M., Lipscomb, J.D. Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 Å resolution. J. Mol. Biol. 244:586-608, 1994.
    • (1994) J. Mol. Biol. , vol.244 , pp. 586-608
    • Ohlendorf, D.H.1    Orville, A.M.2    Lipscomb, J.D.3
  • 79
    • 0029558330 scopus 로고
    • Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center
    • Wilmanns, M., Lappalainen, P., Kelly, M., Sauer-Eriksson, E., Saraste, M. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. Proc. Natl. Acad. Sci. U.S.A. 92:11955-11959, 1995.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11955-11959
    • Wilmanns, M.1    Lappalainen, P.2    Kelly, M.3    Sauer-Eriksson, E.4    Saraste, M.5
  • 80
    • 0028220527 scopus 로고
    • Crystal structure analysis and refinement at 2.15 Å resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus
    • Romero, A., Nar, H., Huber, R., Messerschmidt, A., Kalverda, A.P., Canters, G.W., Durley, R., Mathews, F.S. Crystal structure analysis and refinement at 2.15 Å resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus. J. Mol. Biol. 236:1196-1211, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1196-1211
    • Romero, A.1    Nar, H.2    Huber, R.3    Messerschmidt, A.4    Kalverda, A.P.5    Canters, G.W.6    Durley, R.7    Mathews, F.S.8
  • 81
    • 0021104996 scopus 로고
    • Structure of oxidized poplar plastocyanin at 1.6 Å resolution
    • Guss, J.M., Freeman, H.C. Structure of oxidized poplar plastocyanin at 1.6 Å resolution. J. Mol. Biol. 169:521-563, 1983.
    • (1983) J. Mol. Biol. , vol.169 , pp. 521-563
    • Guss, J.M.1    Freeman, H.C.2
  • 82
    • 0021103759 scopus 로고
    • Structure of azurin from Alcaligenes denitrificans at 2.5 Å resolution
    • Norris, G.E., Anderson, B.F., Baker, E.N. Structure of azurin from Alcaligenes denitrificans at 2.5 Å resolution. J. Mol. Biol. 165:501-521, 1983.
    • (1983) J. Mol. Biol. , vol.165 , pp. 501-521
    • Norris, G.E.1    Anderson, B.F.2    Baker, E.N.3
  • 84
    • 0027096460 scopus 로고
    • Crystal structure of a sweet tasting protein thaumatin I, at 1.65 Å resolution
    • Ogata, C.M., Gordon, P.F., de Vos, A.M., Kim, S.-H. Crystal structure of a sweet tasting protein thaumatin I, at 1.65 Å resolution. J. Mol. Biol. 228:893-908, 1992.
    • (1992) J. Mol. Biol. , vol.228 , pp. 893-908
    • Ogata, C.M.1    Gordon, P.F.2    De Vos, A.M.3    Kim, S.-H.4
  • 85
    • 0022486526 scopus 로고
    • Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467 A
    • Pflugrath, J. W., Wiegand, G., Huber, R., Vértesy, L. Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467 A. J. Mol. Biol. 189:383-386, 1986.
    • (1986) J. Mol. Biol. , vol.189 , pp. 383-386
    • Pflugrath, J.W.1    Wiegand, G.2    Huber, R.3    Vértesy, L.4
  • 86
    • 0017855552 scopus 로고
    • Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin New at 2.0 Å resolution
    • Saul, F.A., Amzel, L.M., Poljak, R.J. Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin New at 2.0 Å resolution. J. Biol. Chem. 253:585-597, 1978.
    • (1978) J. Biol. Chem. , vol.253 , pp. 585-597
    • Saul, F.A.1    Amzel, L.M.2    Poljak, R.J.3
  • 88
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian, D.L., Jones, E.Y., Harlos, K., Stuart, D.I., Davis, S.J. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 2:755-766, 1994.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 89
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase
    • Tainer, J.A., Getzoff, E.D., Beem, K.M., Richardson, J.S., Richardson, D.C. Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160:181-217, 1982.
    • (1982) J. Mol. Biol. , vol.160 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5
  • 90
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
    • Holmgren, A., Brändén, C.-I. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 342:248-251, 1989.
    • (1989) Nature , vol.342 , pp. 248-251
    • Holmgren, A.1    Brändén, C.-I.2
  • 91
    • 0030021265 scopus 로고    scopus 로고
    • The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family
    • Batalia, M.A., Monzingo, A.F., Ernst, S., Roberts, W., Robertus, J.D. The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family. Nature Struct. Biol. 3:19-22, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 19-22
    • Batalia, M.A.1    Monzingo, A.F.2    Ernst, S.3    Roberts, W.4    Robertus, J.D.5
  • 92
    • 0029151455 scopus 로고
    • The structure of satellite panicum mosaic virus at 1.9 Å resolution
    • Ban, N., McPherson, A. The structure of satellite panicum mosaic virus at 1.9 Å resolution. Nature Struct. Biol. 2:882-890, 1995.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 882-890
    • Ban, N.1    McPherson, A.2
  • 93
    • 0027256201 scopus 로고
    • Three-dimensional structure of satellite tobacco mosaic virus at 2.9 Å resolution
    • Larson, S.B., Koszelak, S., Day, J., Greenwood, A., Dodds, J.A., McPherson, A. Three-dimensional structure of satellite tobacco mosaic virus at 2.9 Å resolution. J. Mol. Biol. 231:375-391, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 375-391
    • Larson, S.B.1    Koszelak, S.2    Day, J.3    Greenwood, A.4    Dodds, J.A.5    McPherson, A.6
  • 94
    • 0028774531 scopus 로고
    • The three-dimensional structure of PNGase F, a glycosyl asparaginase from Flavobacterium meningosepticum
    • Norris, G.E., Stillman, T.J., Anderson, B.F., Baker, E.N. The three-dimensional structure of PNGase F, a glycosyl asparaginase from Flavobacterium meningosepticum. Structure 2:1049-1059, 1994.
    • (1994) Structure , vol.2 , pp. 1049-1059
    • Norris, G.E.1    Stillman, T.J.2    Anderson, B.F.3    Baker, E.N.4
  • 96
    • 0027953618 scopus 로고
    • The refined three-dimensional structure of an insect virus at 2.8 Å resolution
    • Wery, J.-P., Reddy, V.S., Hosur, M.V., Johnson, J.E. The refined three-dimensional structure of an insect virus at 2.8 Å resolution. J. Mol. Biol. 235:565-568, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 565-568
    • Wery, J.-P.1    Reddy, V.S.2    Hosur, M.V.3    Johnson, J.E.4
  • 98
    • 0023645549 scopus 로고
    • Refined structure of southern bean mosaic virus at 2.9 Å resolution
    • Silva, A.M., Rossmann, M.G. Refined structure of southern bean mosaic virus at 2.9 Å resolution. J. Mol. Biol. 197:69-87, 1987.
    • (1987) J. Mol. Biol. , vol.197 , pp. 69-87
    • Silva, A.M.1    Rossmann, M.G.2
  • 100
    • 0029878731 scopus 로고    scopus 로고
    • Structure of human β-glucuronidase reveals candidate lysosomal targeting and active-site motifs
    • Jain, S., Drendel, W.B., Chen, Z., Mathews, F.S., Sly, W.S., Grubb, J.H. Structure of human β-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nature Struct. Biol. 3:375-381, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 375-381
    • Jain, S.1    Drendel, W.B.2    Chen, Z.3    Mathews, F.S.4    Sly, W.S.5    Grubb, J.H.6
  • 102
    • 0028773048 scopus 로고
    • NMR-derived three-dimensional solution structure of protein S complexed with calcium
    • Bagby, S., Harvey, T.S., Eagle, S.G., Inouye, S., Ikura, M. NMR-derived three-dimensional solution structure of protein S complexed with calcium. Structure 2:107-122, 1994.
    • (1994) Structure , vol.2 , pp. 107-122
    • Bagby, S.1    Harvey, T.S.2    Eagle, S.G.3    Inouye, S.4    Ikura, M.5
  • 103
    • 0027296794 scopus 로고
    • Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution
    • Qian, M., Haser, R., Payan, F. Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 231:785-799, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 785-799
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 107
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., Gorina, S., Jeffrey, P.D., Pavletich, N.P. Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations. Science 265:346-355, 1994.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 108
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez, S.E., Huang, D., Szczepaniak, A., Cramer, W.A., Smith, J.L. Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2:95-105, 1994.
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 110
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with Mg ATP and peptide inhibitor
    • Zheng, J., Knighton, D.R., Ten Eyck, L.F., Karlsson, R., Xuong, N., Taylor, S.S., Sowadski, J.M. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with Mg ATP and peptide inhibitor. Biochemistry 32:2154-2161, 1993.
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.5    Taylor, S.S.6    Sowadski, J.M.7
  • 111
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen, D.J., Noble, M.E.M., Garman, E.F., Papageorgiou, A.C., Johnson, L.N. Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product. Structure 3:467-482, 1995.
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.M.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 112
    • 0030585119 scopus 로고    scopus 로고
    • Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly
    • Lee, S., Owen, K.E., Choi, H.-K., Lee, H., Lu, G., Wengler, G., Brown, D.T., Rossmann, M.G., Kuhn, K.J. Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly. Structure 4:531-541, 1996.
    • (1996) Structure , vol.4 , pp. 531-541
    • Lee, S.1    Owen, K.E.2    Choi, H.-K.3    Lee, H.4    Lu, G.5    Wengler, G.6    Brown, D.T.7    Rossmann, M.G.8    Kuhn, K.J.9
  • 113
    • 0028841677 scopus 로고
    • A potential catalytic site revealed by the 1.7-Å crystal structure of the amino-terminal signalling domain of Sonic hedgehog
    • Tanaka Hall, T.M., Porter, J.A., Beachy, P.A., Leahy, D.J. A potential catalytic site revealed by the 1.7-Å crystal structure of the amino-terminal signalling domain of Sonic hedgehog. Nature 378:212-216, 1995.
    • (1995) Nature , vol.378 , pp. 212-216
    • Tanaka Hall, T.M.1    Porter, J.A.2    Beachy, P.A.3    Leahy, D.J.4
  • 115
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison, C.J., Bohm, A.A., Nelson, H.C.M. Crystal structure of the DNA binding domain of the heat shock transcription factor. Science 263:224-227, 1994.
    • (1994) Science , vol.263 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.M.3
  • 116
    • 0029131487 scopus 로고
    • Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution
    • Momany, C., Ernst, S., Ghosh, R., Chang, N.-L., Hackert, M.L. Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution. J. Mol. Biol. 252:643-655, 1995.
    • (1995) J. Mol. Biol. , vol.252 , pp. 643-655
    • Momany, C.1    Ernst, S.2    Ghosh, R.3    Chang, N.-L.4    Hackert, M.L.5
  • 117
    • 0029001623 scopus 로고
    • Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator
    • Endrizzi, J.A., Cronk, J.D., Wang, W., Crabtree, G.R., Alber, T. Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Science 268, 556-559, 1995.
    • (1995) Science , vol.268 , pp. 556-559
    • Endrizzi, J.A.1    Cronk, J.D.2    Wang, W.3    Crabtree, G.R.4    Alber, T.5
  • 118
    • 0027273988 scopus 로고
    • Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coll: A new type of proteolytic enzyme
    • Roderick, S.L., Matthews, B.W. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coll: A new type of proteolytic enzyme. Biochemistry 32:3907-3912, 1993.
    • (1993) Biochemistry , vol.32 , pp. 3907-3912
    • Roderick, S.L.1    Matthews, B.W.2
  • 119
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose 1,5-biphosphate carboxylase from spinach at 2.4 Å resolution. Subunit interactions and active site
    • Knight, S., Andersson, I., Brändén, C.-I. Crystallographic analysis of ribulose 1,5-biphosphate carboxylase from spinach at 2.4 Å resolution. Subunit interactions and active site. J. Mol. Biol. 215:113-160, 1990.
    • (1990) J. Mol. Biol. , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Brändén, C.-I.3
  • 120
    • 0029200246 scopus 로고
    • 2Å resolution structure of DppA, a periplasmic dipeptide transport/ chemosensory receptor
    • Nickitenko, A.V., Trakhanov, S., Quiocho, F.A. 2Å resolution structure of DppA, a periplasmic dipeptide transport/ chemosensory receptor. Biochemistry 34:16585-16595, 1995.
    • (1995) Biochemistry , vol.34 , pp. 16585-16595
    • Nickitenko, A.V.1    Trakhanov, S.2    Quiocho, F.A.3
  • 121
    • 0029670095 scopus 로고    scopus 로고
    • Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli
    • Van Duyne, G.D., Ghosh, G., Maas, W.K., Sigler, P.B. Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli. J. Mol. Biol. 256:377-391, 1996.
    • (1996) J. Mol. Biol. , vol.256 , pp. 377-391
    • Van Duyne, G.D.1    Ghosh, G.2    Maas, W.K.3    Sigler, P.B.4
  • 123
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0Å resolution
    • Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., Katsube, Y. Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0Å resolution. J. Mol. Biol. 229:1083-1100, 1993.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1    Kato, H.2    Hata, Y.3    Nishioka, T.4    Kimura, A.5    Oda, J.6    Katsube, Y.7
  • 124
    • 0029645414 scopus 로고
    • Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase
    • Georgiadis, M.M., Jessen, S.M., Ogata, C.M., Telesnitsky, A., Goff, S.P., Hendrickson, W.A. Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase. Structure 3:879-892, 1995.
    • (1995) Structure , vol.3 , pp. 879-892
    • Georgiadis, M.M.1    Jessen, S.M.2    Ogata, C.M.3    Telesnitsky, A.4    Goff, S.P.5    Hendrickson, W.A.6
  • 125
    • 0023660840 scopus 로고
    • Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli
    • Kim, K.H., Pan, Z., Honzatko, R.B., Ke, H., Lipscomb, W.N. Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli. J. Mol. Biol. 196:853-875, 1987.
    • (1987) J. Mol. Biol. , vol.196 , pp. 853-875
    • Kim, K.H.1    Pan, Z.2    Honzatko, R.B.3    Ke, H.4    Lipscomb, W.N.5
  • 127
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein Hor from Bacillus subtilis at 2.0-Å resolution
    • Herzberg, O., Reddy, P., Sutrina, S., Saier, M.H., Reizer, J., Kapadia, G. Structure of the histidine-containing phosphocarrier protein Hor from Bacillus subtilis at 2.0-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 89:2499-2503, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2499-2503
    • Herzberg, O.1    Reddy, P.2    Sutrina, S.3    Saier, M.H.4    Reizer, J.5    Kapadia, G.6
  • 128
    • 0015919836 scopus 로고
    • The structure of a bacterial ferredoxin
    • Adman, E.T., Sicker, L.C., Jensen, L.H. The structure of a bacterial ferredoxin. J. Biol. Chem. 248:3987-3996, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3987-3996
    • Adman, E.T.1    Sicker, L.C.2    Jensen, L.H.3
  • 129
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai, K., Oubridge, C., Jessen, T.H., Li, J., Evans, P.R. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature 348:515-520, 1990.
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 131
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • Hegde, R.S., Grossman, S.R., Laimins, L.A., Sigler, P.B. Crystal structure at 1.7 Å of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target. Nature 359:505-512, 1992.
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 132
    • 0026548881 scopus 로고
    • Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation
    • Guasch, A., Coll, M., Avilés, F.X., Huber, R. Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 224:141-157, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 141-157
    • Guasch, A.1    Coll, M.2    Avilés, F.X.3    Huber, R.4
  • 133
    • 0029113242 scopus 로고
    • Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry
    • Krezel, A.M., Kasibhatla, C., Hidalgo, P., MacKinnon, R., Wagner, G. Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry. Protein Sci. 4:1478-1489, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 1478-1489
    • Krezel, A.M.1    Kasibhatla, C.2    Hidalgo, P.3    MacKinnon, R.4    Wagner, G.5
  • 135
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., Popp, D., Holmes, K.C. Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836, 1993.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 137
    • 0028057520 scopus 로고
    • Cytidine deaminase: The 2.3 Å crystal structure of an enzyme: Transition-state analog complex
    • Betts, L., Xiang, S., Short, S.A., Wolfenden, R., Carter, C.W., Jr. Cytidine deaminase: The 2.3 Å crystal structure of an enzyme: Transition-state analog complex. J. Mol. Biol. 235:635-656, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 635-656
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter Jr., C.W.5
  • 139
    • 0023038391 scopus 로고
    • Crystallographic refinement and structure of DNase I at 2 Å resolution
    • Oefner, C., Suck, D. Crystallographic refinement and structure of DNase I at 2 Å resolution. J. Mol. Biol. 192:605-632, 1986.
    • (1986) J. Mol. Biol. , vol.192 , pp. 605-632
    • Oefner, C.1    Suck, D.2
  • 140
    • 0029111710 scopus 로고
    • X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an a helix
    • Biou, V., Shu, F., Ramakrishnan, V. X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an a helix. EMBO J. 14:4056-4064, 1995.
    • (1995) EMBO J. , vol.14 , pp. 4056-4064
    • Biou, V.1    Shu, F.2    Ramakrishnan, V.3
  • 142
    • 0027979546 scopus 로고
    • Crystal structure of a disulfide-linked "trefoil" motif found in a large family of putative growth factors
    • De, A., Brown, D.G., Gorman, M.A., Carr, M., Sanderson, M.R., Freemont, P.S. Crystal structure of a disulfide-linked "trefoil" motif found in a large family of putative growth factors. Proc. Natl. Acad. Sci. U.S.A. 91:1084-1088, 1994.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1084-1088
    • De, A.1    Brown, D.G.2    Gorman, M.A.3    Carr, M.4    Sanderson, M.R.5    Freemont, P.S.6
  • 143
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P.J., Gooch, J.T., Mannherz, H.-G., Weeds, A.G. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364:685-692, 1993.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 144
    • 0023644678 scopus 로고
    • Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 Å resolution
    • Wright, C.S. Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 Å resolution. J. Mol. Biol. 194:501-529, 1987.
    • (1987) J. Mol. Biol. , vol.194 , pp. 501-529
    • Wright, C.S.1
  • 145
    • 0023851488 scopus 로고
    • Iron superoxide dismutase: Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures
    • Carlioz, A., Ludwig, M.L., Stallings, W.C., Fee, J.A., Steinman, H.M., Touati, D. Iron superoxide dismutase: Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. J. Biol. Chem. 263:1555-1562, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1555-1562
    • Carlioz, A.1    Ludwig, M.L.2    Stallings, W.C.3    Fee, J.A.4    Steinman, H.M.5    Touati, D.6
  • 146
    • 0024292275 scopus 로고
    • Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 Å resolution
    • Parker, M.W., Blake, C.C.F. Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 Å resolution. J. Mol. Biol. 199:649-661, 1988.
    • (1988) J. Mol. Biol. , vol.199 , pp. 649-661
    • Parker, M.W.1    Blake, C.C.F.2
  • 147
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar, S., Bugg, C.E., Cook, W.J. Structure of ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194:531-544, 1987.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 148
    • 0026613602 scopus 로고
    • 1.67-Å x-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain
    • Achari, A., Hale, S.P., Howard, A.J., Clore, G.M., Gronenborn, A.M., Hardman, K.D., Whitlow, M. 1.67-Å x-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain. Biochemistry 31:10449-10457, 1992.
    • (1992) Biochemistry , vol.31 , pp. 10449-10457
    • Achari, A.1    Hale, S.P.2    Howard, A.J.3    Clore, G.M.4    Gronenborn, A.M.5    Hardman, K.D.6    Whitlow, M.7
  • 149
    • 0027276877 scopus 로고
    • Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a
    • Gallagher, T., Rozwarski, D.A., Ernst, S.R., Hackert, M.L. Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. J. Mol. Biol. 230: 516-528, 1993.
    • (1993) J. Mol. Biol. , vol.230 , pp. 516-528
    • Gallagher, T.1    Rozwarski, D.A.2    Ernst, S.R.3    Hackert, M.L.4
  • 151
    • 0027236660 scopus 로고
    • Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution
    • Day, C.L., Anderson, B.F., Tweedie, J.W., Baker, E.N. Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution. J. Mol. Biol. 232:1084-1100, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1084-1100
    • Day, C.L.1    Anderson, B.F.2    Tweedie, J.W.3    Baker, E.N.4
  • 152
    • 0029025769 scopus 로고
    • Towards structure-based drug design: Crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 Å resolution
    • Klein, C., Chen, P., Arevalo, J.H., Stura, E.A., Marolewski, A., Warren, M.S., Benkovic, S.J., Wilson, I.A. Towards structure-based drug design: Crystal structure of a multisubstrate adduct complex of glycinamide ribonucleotide transformylase at 1.96 Å resolution. J. Mol. Biol. 249:153-175, 1995.
    • (1995) J. Mol. Biol. , vol.249 , pp. 153-175
    • Klein, C.1    Chen, P.2    Arevalo, J.H.3    Stura, E.A.4    Marolewski, A.5    Warren, M.S.6    Benkovic, S.J.7    Wilson, I.A.8
  • 153
    • 0029967678 scopus 로고    scopus 로고
    • Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution
    • Arjunan, P., Umland, T., Dyda, F., Swaminathan, S., Furey, W., Sax, M., Farrenkopf, B., Gao, Y., Zhang, D., Jordan, F. Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution. J. Mol. Biol. 256:590-600, 1996.
    • (1996) J. Mol. Biol. , vol.256 , pp. 590-600
    • Arjunan, P.1    Umland, T.2    Dyda, F.3    Swaminathan, S.4    Furey, W.5    Sax, M.6    Farrenkopf, B.7    Gao, Y.8    Zhang, D.9    Jordan, F.10
  • 154
    • 0023644310 scopus 로고
    • Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution
    • Skarzysnki, T., Moody, P.C.E., Wonacott, A.J. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution. J. Mol. Biol. 193:171-187, 1987.
    • (1987) J. Mol. Biol. , vol.193 , pp. 171-187
    • Skarzysnki, T.1    Moody, P.C.E.2    Wonacott, A.J.3
  • 155
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • Vrielink, A., Ruger, W., Driessen, H.P.C., Freemont, P.S. Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J. 13:3413-3422, 1994.
    • (1994) EMBO J. , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Ruger, W.2    Driessen, H.P.C.3    Freemont, P.S.4
  • 156
    • 0028773899 scopus 로고
    • Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism
    • Adams, M.J., Ellis, G.H., Cover, S., Naylor, C.E., Phillips, C. Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism. Structure 2:651-668, 1994.
    • (1994) Structure , vol.2 , pp. 651-668
    • Adams, M.J.1    Ellis, G.H.2    Cover, S.3    Naylor, C.E.4    Phillips, C.5
  • 157
    • 0024383933 scopus 로고
    • The structure of aconitase
    • Robbins, A.H., Stout, C.D. The structure of aconitase. Proteins 5:289-312, 1989.
    • (1989) Proteins , vol.5 , pp. 289-312
    • Robbins, A.H.1    Stout, C.D.2
  • 159
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution
    • Bauer, A.J., Rayment, I., Frey, P.A., Holden, H.M. The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution. Proteins 12:372-381, 1992.
    • (1992) Proteins , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 160
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3αa,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases
    • Ghosh, D., Wawrzak, Z., Weeks, C.M., Duax, W.L., Erman, M. The refined three-dimensional structure of 3αa,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure 2:629-640, 1994.
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 162
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka, N., Nonaka, T., Nakanishi, M., Deyashiki, Y., Hara, A., Mitsui, Y. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4:33-45, 1996.
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 163
    • 0029645410 scopus 로고
    • Common themes in redox chemistry emerge from the x-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase
    • Rafferty, J.B., Simon, J.W., Baldock, C., Artymiuk, P.J., Baker, P.J., Stuitje, A.R., Slabas, A.R., Rice, D.W. Common themes in redox chemistry emerge from the x-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase. Structure 3:927-938, 1995.
    • (1995) Structure , vol.3 , pp. 927-938
    • Rafferty, J.B.1    Simon, J.W.2    Baldock, C.3    Artymiuk, P.J.4    Baker, P.J.5    Stuitje, A.R.6    Slabas, A.R.7    Rice, D.W.8
  • 164
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • + reductase: Prototype for a structurally novel flavoenzyme family. Science 251:60-66, 1991.
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 165
    • 0028812143 scopus 로고
    • Crystal structure of DNA photolyase from Escherichia coli
    • Park, H.-W., Kim, S.-T., Sancar, A., Deisenhofer, J. Crystal structure of DNA photolyase from Escherichia coli. Science 268:1866-1672, 1995.
    • (1995) Science , vol.268 , pp. 1866-11672
    • Park, H.-W.1    Kim, S.-T.2    Sancar, A.3    Deisenhofer, J.4
  • 166
    • 0029643793 scopus 로고
    • Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase
    • Doublie, S., Bricogne, G., Gilmore, C., Carter, C.W., Jr. Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure 3:17-31, 1995.
    • (1995) Structure , vol.3 , pp. 17-31
    • Doublie, S.1    Bricogne, G.2    Gilmore, C.3    Carter Jr., C.W.4
  • 167
    • 0027093793 scopus 로고
    • Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]
    • Correll, C.C., Batie, C.J., Ballou, D.P., Ludwig, M.L. Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258:1604-1610, 1992.
    • (1992) Science , vol.258 , pp. 1604-1610
    • Correll, C.C.1    Batie, C.J.2    Ballou, D.P.3    Ludwig, M.L.4
  • 168
    • 0027338134 scopus 로고
    • Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-L-methionine
    • Cheng, X., Kumar, S., Posfai, J., Pflugrath, J.W., Roberts, R.J. Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-L-methionine. Cell 74:299-307, 1993.
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Posfai, J.3    Pflugrath, J.W.4    Roberts, R.J.5
  • 169
    • 0027444661 scopus 로고
    • Crystal structure of adenylosuccinate synthetase from Escherichia coli: Evidence for convergent evolution of GTP-binding domains
    • Poland, B.W., Silva, M.M., Serra, M.A., Cho, Y., Kim, K.H., Harris, E.M.S., Honzatko, R.B. Crystal structure of adenylosuccinate synthetase from Escherichia coli: Evidence for convergent evolution of GTP-binding domains. J. Biol. Chem. 268:25334-25342, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25334-25342
    • Poland, B.W.1    Silva, M.M.2    Serra, M.A.3    Cho, Y.4    Kim, K.H.5    Harris, E.M.S.6    Honzatko, R.B.7
  • 170
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner, C., D'Arcy, A., Winkler, F.K. Crystal structure of human dihydrofolate reductase complexed with folate. Eur. J. Biochem. 174:377-385, 1988.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 377-385
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3
  • 171
    • 0029645125 scopus 로고
    • Crystal structure of Escherichia coli pyruvate kinase type I: Molecular basis of the allosteric transition
    • Mattevi, A., Valentini, G., Rizzi, M., Speranza, M.L., Bolognesi, M., Coda, A. Crystal structure of Escherichia coli pyruvate kinase type I: Molecular basis of the allosteric transition. Structure 3:729-741, 1995.
    • (1995) Structure , vol.3 , pp. 729-741
    • Mattevi, A.1    Valentini, G.2    Rizzi, M.3    Speranza, M.L.4    Bolognesi, M.5    Coda, A.6
  • 173
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase MTaq I in complex with the cofactor S-adenosylmethionine
    • Labahn, J., Granzin, J., Schluckebier, G., Robinson, D.P., Jack, W.E., Schildkraut, I. Three-dimensional structure of the adenine-specific DNA methyltransferase MTaq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. U.S.A. 91:10957-10961, 1994.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10957-10961
    • Labahn, J.1    Granzin, J.2    Schluckebier, G.3    Robinson, D.P.4    Jack, W.E.5    Schildkraut, I.6
  • 174
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • Vidgren, J., Svensson, L.A., Liljas, A. Crystal structure of catechol O-methyltransferase. Nature 368:354-358, 1994.
    • (1994) Nature , vol.368 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 175
    • 0019880506 scopus 로고
    • Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution
    • Eklund, H., Samama, J.-P., Wallen, L., Brändén, C.-I., Åkerson, Å., Jones, T.A. Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution. J. Mol. Biol. 146:561-587, 1981.
    • (1981) J. Mol. Biol. , vol.146 , pp. 561-587
    • Eklund, H.1    Samama, J.-P.2    Wallen, L.3    Brändén, C.-I.4    Åkerson, Å.5    Jones, T.A.6
  • 176
    • 0346054921 scopus 로고
    • Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-Å resolution
    • Ke, H.-M., Honzatko, R.B., Lipscomb, W.N. Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 81:4037-4040, 1984.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4037-4040
    • Ke, H.-M.1    Honzatko, R.B.2    Lipscomb, W.N.3
  • 177
    • 0028773470 scopus 로고
    • The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum
    • John, J., Crennell, S.J., Hough, D.W., Danson, M.J., Taylor, G.L. The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum. Structure 2:385-393, 1994.
    • (1994) Structure , vol.2 , pp. 385-393
    • John, J.1    Crennell, S.J.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 178
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
    • Tesmer, J.J.G., Klem, T.J., Deras, M.L., Davisson, V.J., Smith, J.L. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nature Struct. Biol. 3:74-86, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 74-86
    • Tesmer, J.J.G.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5
  • 179
    • 0028278602 scopus 로고
    • Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution
    • Goldberg, J.D., Yoshida, T., Brick, P. Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution. J. Mol. Biol. 236:1123-1140, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1123-1140
    • Goldberg, J.D.1    Yoshida, T.2    Brick, P.3
  • 180
    • 0030584680 scopus 로고    scopus 로고
    • Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase
    • Stoll, V.S., Kimber, M.S., Pai, E.F. Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase. Structure 4:437-447, 1996.
    • (1996) Structure , vol.4 , pp. 437-447
    • Stoll, V.S.1    Kimber, M.S.2    Pai, E.F.3
  • 181
    • 0029665054 scopus 로고    scopus 로고
    • The 1.85 Å structure of vaccinia protein VP39: A bifunctional enzyme that participates in the modification of both mRNA ends
    • Hodel, A.E., Gershon, P.D., Shi, X., Quiocho, F.A. The 1.85 Å structure of vaccinia protein VP39: A bifunctional enzyme that participates in the modification of both mRNA ends. Cell 85:247-256, 1996.
    • (1996) Cell , vol.85 , pp. 247-256
    • Hodel, A.E.1    Gershon, P.D.2    Shi, X.3    Quiocho, F.A.4
  • 182
    • 0029646095 scopus 로고
    • Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution
    • Oliva, G., Fontes, M.R.M., Garratt, R.C., Altamirano, M.M., Calcagno, M.L., Horjales, E. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 Å resolution. Structure 3:1323-1332, 1995.
    • (1995) Structure , vol.3 , pp. 1323-1332
    • Oliva, G.1    Fontes, M.R.M.2    Garratt, R.C.3    Altamirano, M.M.4    Calcagno, M.L.5    Horjales, E.6
  • 183
    • 0029645116 scopus 로고
    • A role for quaternary structure in the substrate specificity of leucine dehydrogenase
    • Baker, P.J., Turnbull, A.P., Sedelnikova, S.E., Stillman, T.J., Rice, D.W. A role for quaternary structure in the substrate specificity of leucine dehydrogenase. Structure 3:693-705, 1995.
    • (1995) Structure , vol.3 , pp. 693-705
    • Baker, P.J.1    Turnbull, A.P.2    Sedelnikova, S.E.3    Stillman, T.J.4    Rice, D.W.5
  • 184
    • 0027479683 scopus 로고
    • Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase
    • Muller, Y.A., Schulz, G.E. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 259: 965-967, 1993.
    • (1993) Science , vol.259 , pp. 965-967
    • Muller, Y.A.1    Schulz, G.E.2
  • 186
    • 0026706804 scopus 로고
    • Crystal structure of Escherichia coli malate dehydrogenase: A complex of the apoenzyme and citrate at 1.87 Å resolution
    • Hall, M.D., Levitt, D.G., Banaszak, L.J. Crystal structure of Escherichia coli malate dehydrogenase: A complex of the apoenzyme and citrate at 1.87 Å resolution. J. Mol. Biol. 226:867-882, 1992.
    • (1992) J. Mol. Biol. , vol.226 , pp. 867-882
    • Hall, M.D.1    Levitt, D.G.2    Banaszak, L.J.3
  • 187
    • 0029113652 scopus 로고
    • Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 Å resolution: An example of strong asymmetry between subunits
    • Niefind, K., Hecht, H.-J., Schomburg, D. Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 Å resolution: An example of strong asymmetry between subunits. J. Mol. Biol. 251:256-281, 1995.
    • (1995) J. Mol. Biol. , vol.251 , pp. 256-281
    • Niefind, K.1    Hecht, H.-J.2    Schomburg, D.3
  • 188
    • 0026483887 scopus 로고
    • Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 Å resolution
    • Romao, M.J., Turk, D., Gomis-Röth, F.-X., Huber, R., Schumacher, G., Müllering, H., Rüssmann, L. Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 Å resolution. J. Mol. Biol. 226:1111-1130, 1992.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1111-1130
    • Romao, M.J.1    Turk, D.2    Gomis-Röth, F.-X.3    Huber, R.4    Schumacher, G.5    Müllering, H.6    Rüssmann, L.7
  • 189
    • 0017158856 scopus 로고
    • Structure of glycogen phosphorylase a at 3.0 Å resolution and its ligand binding sites at 6 Å
    • Fletterick, R.J., Sygusch, J., Semple, H., Madsen, N.B. Structure of glycogen phosphorylase a at 3.0 Å resolution and its ligand binding sites at 6 Å. J. Biol. Chem. 251:6142-6146, 1976.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6142-6146
    • Fletterick, R.J.1    Sygusch, J.2    Semple, H.3    Madsen, N.B.4
  • 190
    • 0026500416 scopus 로고
    • The structure of the E. coli rec A protein monomer and polymer
    • Story, R.M., Weber, I.T., Steitz, T.A. The structure of the E. coli rec A protein monomer and polymer. Nature 355:318-325, 1992.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 193
    • 0018177366 scopus 로고
    • Structure of bovine liver rhodanese. I. Structure determination at 2.5 Å resolution and a comparison of the conformation and sequence of its two domains
    • Ploegman, J.H., Drent, G., Kalk, K.H., Hol, W.G.J. Structure of bovine liver rhodanese. I. Structure determination at 2.5 Å resolution and a comparison of the conformation and sequence of its two domains. J. Mol. Biol. 123:557-594, 1978.
    • (1978) J. Mol. Biol. , vol.123 , pp. 557-594
    • Ploegman, J.H.1    Drent, G.2    Kalk, K.H.3    Hol, W.G.J.4
  • 194
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii
    • Kim, J., Rees, D.C. Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. Nature 360:553-560, 1992.
    • (1992) Nature , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 195
    • 0028174351 scopus 로고
    • The 2.8Å crystal structure of peroxisomal 3-ketoacyl-Coa thiolase of Saccharomyces cerevisiae: A five-layered αβαβα structure constructed from two core domains of identical topology
    • Mathieu, M., Zeelen, J.Ph., Pauptit, R.A., Erdmann, R., Kunau, W.-H., Wierenga, R.K. The 2.8Å crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: A five-layered αβαβα structure constructed from two core domains of identical topology. Structure 2:797-808, 1994.
    • (1994) Structure , vol.2 , pp. 797-808
    • Mathieu, M.1    Zeelen, J.Ph.2    Pauptit, R.A.3    Erdmann, R.4    Kunau, W.-H.5    Wierenga, R.K.6
  • 196
    • 0028297538 scopus 로고
    • Crystalline mitochondrial aspartate aminotransferase exists in only two conformations
    • Hohenester, E., Jansonius, J.N. Crystalline mitochondrial aspartate aminotransferase exists in only two conformations. J. Mol. Biol. 236:963-968, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 963-968
    • Hohenester, E.1    Jansonius, J.N.2
  • 198
    • 0028921425 scopus 로고
    • Structural motifs for pyridoxal-5-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase
    • Momany, C., Ghosh, R., Hackert, M.L. Structural motifs for pyridoxal-5-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase. Protein Sci. 4:849-854, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 849-854
    • Momany, C.1    Ghosh, R.2    Hackert, M.L.3
  • 199
    • 0019486502 scopus 로고
    • Structure of the L-arabinose-binding protein from Escherichia coli at 2.4 Å resolution
    • Gilliland, G.L., Quiocho, F.A. Structure of the L-arabinose-binding protein from Escherichia coli at 2.4 Å resolution. J. Mol. Biol. 146:341-362, 1981.
    • (1981) J. Mol. Biol. , vol.146 , pp. 341-362
    • Gilliland, G.L.1    Quiocho, F.A.2
  • 200
    • 0029868999 scopus 로고    scopus 로고
    • Crystal structure of the rat liver fructose-2,6-biphosphatase based on selenomethionine multiwavelength anomalous dispersion phases
    • Lee, Y.-H., Ogata, C., Pflugrath, J.W., Levitt, D.G., Sarma, R., Banaszak, L.J., Pilkis, S.J. Crystal structure of the rat liver fructose-2,6-biphosphatase based on selenomethionine multiwavelength anomalous dispersion phases. Biochemistry 35:6010-6019, 1996.
    • (1996) Biochemistry , vol.35 , pp. 6010-6019
    • Lee, Y.-H.1    Ogata, C.2    Pflugrath, J.W.3    Levitt, D.G.4    Sarma, R.5    Banaszak, L.J.6    Pilkis, S.J.7
  • 201
    • 0028607139 scopus 로고
    • Crystal structure of Ami C: The controller of transcription antitermination in the amidase operon of Pseudomonas aeruginosa
    • Pearl, L., O'Hara, B., Drew, R., Wilson, S. Crystal structure of Ami C: The controller of transcription antitermination in the amidase operon of Pseudomonas aeruginosa. EMBO J. 13:5810-5817, 1994.
    • (1994) EMBO J. , vol.13 , pp. 5810-5817
    • Pearl, L.1    O'Hara, B.2    Drew, R.3    Wilson, S.4
  • 202
    • 0024563996 scopus 로고
    • Periplasmic binding protein structure and function: Refined x-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine
    • Sack, J.S., Saper, M.A., Quiocho, F.A. Periplasmic binding protein structure and function: Refined x-ray structures of the leucine/isoleucine/valine-binding protein and its complex with leucine. J. Mol. Biol. 206:171-191, 1989.
    • (1989) J. Mol. Biol. , vol.206 , pp. 171-191
    • Sack, J.S.1    Saper, M.A.2    Quiocho, F.A.3
  • 203
    • 0028083309 scopus 로고
    • The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP
    • Eads, J.C., Scapin, G., Xu, Y., Grubmeyer, C., Sacchettini, J.C. The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell 78:325-334, 1994.
    • (1994) Cell , vol.78 , pp. 325-334
    • Eads, J.C.1    Scapin, G.2    Xu, Y.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 204
    • 0026544877 scopus 로고
    • 5a refined at 1.9 Å resolution: A model for a catalytic transition state
    • 5A refined at 1.9 Å resolution: A model for a catalytic transition state. J. Mol. Biol. 224:159-177, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 159-177
    • Müller, C.W.1    Schulz, G.E.2
  • 205
    • 0024215739 scopus 로고
    • Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
    • Shirakihara, Y., Evans, P.R. Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. J. Mol. Biol. 204:973-994, 1988.
    • (1988) J. Mol. Biol. , vol.204 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.R.2
  • 206
    • 0028773464 scopus 로고
    • Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 Å resolution
    • Huang, W., Lindqvist, Y., Schneider, G., Gibson, K.J., Flint, D., Lorimer, G. Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 Å resolution. Structure 2:407-414, 1994.
    • (1994) Structure , vol.2 , pp. 407-414
    • Huang, W.1    Lindqvist, Y.2    Schneider, G.3    Gibson, K.J.4    Flint, D.5    Lorimer, G.6
  • 208
    • 0024278240 scopus 로고
    • The 2 Å resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium
    • Pflugrath, J.W., Quiocho, F.A. The 2 Å resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium. J. Mol. Biol. 200: 163-180, 1988.
    • (1988) J. Mol. Biol. , vol.200 , pp. 163-180
    • Pflugrath, J.W.1    Quiocho, F.A.2
  • 209
    • 0026321096 scopus 로고
    • Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7 Å resolution
    • Kang, C.-H., Shin, W.-C., Yamagata, Y., Gokcen, S., Ames, G.F.-L., Kim, S.-H. Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7 Å resolution. J. Biol. Chem. 266: 23893-23899, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23893-23899
    • Kang, C.-H.1    Shin, W.-C.2    Yamagata, Y.3    Gokcen, S.4    Ames, G.F.-L.5    Kim, S.-H.6
  • 212
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
    • Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y., Oshima, T. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution. J. Mol. Biol. 222:725-738, 1991.
    • (1991) J. Mol. Biol. , vol.222 , pp. 725-738
    • Imada, K.1    Sato, M.2    Tanaka, N.3    Katsube, Y.4    Matsuura, Y.5    Oshima, T.6
  • 214
    • 0028175417 scopus 로고
    • Refinement of αδ resolvase reveals a strikingly flexible molecule
    • Rice, P.A., Steitz, T.A. Refinement of αδ resolvase reveals a strikingly flexible molecule. Structure 2:371-384, 1994.
    • (1994) Structure , vol.2 , pp. 371-384
    • Rice, P.A.1    Steitz, T.A.2
  • 216
    • 0025160386 scopus 로고
    • Crystal structure of fructose-1,6-biphosphatase complexed with fructose 6-phosphate, AMP, and magnesium
    • Ke, H., Zhang, Y., Lipscomb, W.N. Crystal structure of fructose-1,6-biphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247, 1990.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5243-5247
    • Ke, H.1    Zhang, Y.2    Lipscomb, W.N.3
  • 217
    • 0026493674 scopus 로고
    • Structure of inositol monophosphatase, the putative target of lithium therapy
    • Bone, R., Springer, J.P., Atack, J.R. Structure of inositol monophosphatase, the putative target of lithium therapy. Proc. Natl. Acad. Sci. U.S.A. 89:10031-10035, 1992.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10031-10035
    • Bone, R.1    Springer, J.P.2    Atack, J.R.3
  • 218
    • 0017709121 scopus 로고
    • Structure of the semiquinone form of flavodoxin from Clostridium MP: Extension of 1.8 Å resolution and some comparisons with the oxidized state
    • Smith, W.W., Burnett, R.M., Darling, G.D., Ludwig, M.L. Structure of the semiquinone form of flavodoxin from Clostridium MP: Extension of 1.8 Å resolution and some comparisons with the oxidized state. J. Mol. Biol. 117:195-225, 1977.
    • (1977) J. Mol. Biol. , vol.117 , pp. 195-225
    • Smith, W.W.1    Burnett, R.M.2    Darling, G.D.3    Ludwig, M.L.4
  • 219
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock, A.M., Mottonen, J.M., Stock, J.B., Schutt, C.E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337:745-749, 1989.
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 220
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • Pai, E.F., Kabsch, W., Krengel, U., Holmes, K.C., John, J., Wittinghofer, A. Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341:209-214, 1989.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 221
    • 0027340581 scopus 로고
    • The 1.7 Å refined x-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium
    • Zou, J., Flocco, M.M., Mowbray, S.L. The 1.7 Å refined x-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J. Mol. Biol. 233:739-752, 1993.
    • (1993) J. Mol. Biol. , vol.233 , pp. 739-752
    • Zou, J.1    Flocco, M.M.2    Mowbray, S.L.3
  • 223
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glucosylase
    • Savva, R., McAuley-Hecht, K., Brown, T., Pearl, L. The structural basis of specific base-excision repair by uracil-DNA glucosylase. Nature 373:487-493, 1995.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 226
    • 0028969678 scopus 로고
    • The metzincins: Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stocker, W., Grams, F., Baumann, U., Reinemer, P., Gomis-Ruth, F.-X., McKay, D.B., Bode, W. The metzincins: topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4:824-840, 1995.
    • (1995) Protein Sci. , vol.4 , pp. 824-840
    • Stocker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.-X.5    McKay, D.B.6    Bode, W.7
  • 227
    • 0029091055 scopus 로고
    • Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus
    • Logan, D.T., Mazauric, M.-H., Kern, D., Moras, D. Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. EMBO J. 14:4156-4167, 1995.
    • (1995) EMBO J. , vol.14 , pp. 4156-4167
    • Logan, D.T.1    Mazauric, M.-H.2    Kern, D.3    Moras, D.4
  • 229
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti, S.K., LeMaster, D.M., Eklund, H. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J. Mol. Biol. 212:167-184, 1990.
    • (1990) J. Mol. Biol. , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 231
    • 0027280086 scopus 로고
    • Refined x-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism
    • Verschueren, K.H.G., Franken, S.M., Rozeboom, H.J., Kalk, K.H., Dijkstra, B.W. Refined x-ray structures of haloalkane dehalogenase at pH 6.2 and pH 8.2 and implications for the reaction mechanism. J. Mol. Biol. 232:856-872, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 856-872
    • Verschueren, K.H.G.1    Franken, S.M.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 232
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., Silman, I. Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein. Science 253:872-879, 1991.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 234
    • 0025160881 scopus 로고
    • Refined structure of dienelactone hydrolase at 1.8 Å
    • Pathak, D., Ollis, D. Refined structure of dienelactone hydrolase at 1.8 Å. J. Mol. Biol. 214:497-525, 1990.
    • (1990) J. Mol. Biol. , vol.214 , pp. 497-525
    • Pathak, D.1    Ollis, D.2
  • 235
    • 0028483211 scopus 로고
    • The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold
    • Hecht, H.J., Sobek, H., Haag, T., Pfeifer, O., van Peie, K.-H. The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold. Nature Struct. Biol. 1:532-537, 1994.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 532-537
    • Hecht, H.J.1    Sobek, H.2    Haag, T.3    Pfeifer, O.4    Van Peie, K.-H.5
  • 236
    • 0029645906 scopus 로고
    • Three-dimensional structure of the human 'protective protein': Structure of the precursor form suggests a complex activation mechanism
    • Rudenko, G., Bonten, E., d'Azzo, A., Hol, W.G.J. Three-dimensional structure of the human 'protective protein': Structure of the precursor form suggests a complex activation mechanism. Structure 3:1249-1259, 1995.
    • (1995) Structure , vol.3 , pp. 1249-1259
    • Rudenko, G.1    Bonten, E.2    D'Azzo, A.3    Hol, W.G.J.4
  • 237
    • 0026787333 scopus 로고
    • Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution
    • Liao, D.-I., Breddam, K., Sweet, R.M., Bullock, T., Remington, S.J. Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution. Biochemistry 31:9796-9812, 1992.
    • (1992) Biochemistry , vol.31 , pp. 9796-9812
    • Liao, D.-I.1    Breddam, K.2    Sweet, R.M.3    Bullock, T.4    Remington, S.J.5
  • 238
    • 0026602711 scopus 로고
    • Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin
    • Burley, S.K., David, P.R., Sweet, R.M., Taylor, A., Lipscomb, W.N. Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 224:113-140, 1992.
    • (1992) J. Mol. Biol. , vol.224 , pp. 113-140
    • Burley, S.K.1    David, P.R.2    Sweet, R.M.3    Taylor, A.4    Lipscomb, W.N.5
  • 239
    • 0021095532 scopus 로고
    • Refined crystal structure of carboxypeptidase a at 1.54 Å resolution
    • Rees, D.C., Lewis, M., Lipscomb, W.N. Refined crystal structure of carboxypeptidase A at 1.54 Å resolution. J. Mol. Biol. 168:367-387, 1983.
    • (1983) J. Mol. Biol. , vol.168 , pp. 367-387
    • Rees, D.C.1    Lewis, M.2    Lipscomb, W.N.3
  • 240
    • 0026355156 scopus 로고
    • Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase
    • Derewenda, Z.S., Cambillau, C. Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase. J. Biol. Chem. 266:23112-23119, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23112-23119
    • Derewenda, Z.S.1    Cambillau, C.2
  • 241
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomschy, A., Jaenicke, R. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246:511-521, 1995.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 242
    • 0025974401 scopus 로고
    • Structure of α-α hairpins with short connections
    • Efimov, A.V. Structure of α-α hairpins with short connections. Protein Eng. 4:245-250, 1991.
    • (1991) Protein Eng. , vol.4 , pp. 245-250
    • Efimov, A.V.1
  • 243
    • 0023479421 scopus 로고
    • Why do globular proteins fit the limited set of folding patterns?
    • Finkelstein, A.V., Ptitsyn, O.B. Why do globular proteins fit the limited set of folding patterns? Prog. Biophys. Mol. Biol. 50:171-190, 1987.
    • (1987) Prog. Biophys. Mol. Biol. , vol.50 , pp. 171-190
    • Finkelstein, A.V.1    Ptitsyn, O.B.2
  • 244
    • 0027122748 scopus 로고
    • Proteins. One thousand families for the molecular biologist
    • Chothia, C., Proteins. One thousand families for the molecular biologist. Nature 387:543-544, 1992.
    • (1992) Nature , vol.387 , pp. 543-544
    • Chothia, C.1
  • 245
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera, A.R., Blanco, F.J., Serrano, L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247:670-681, 1995.
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 246
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • Viguera, A.R., Serrano, L., Wilmanns, M. Different folding transition states may result in the same native structure. Nature Struct. Bio.3:874-880, 1996.
    • (1996) Nature Struct. Bio. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 247
    • 0030342680 scopus 로고    scopus 로고
    • Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink
    • Barbar, E., Barany, G., Woodward, C. Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink. Folding Design 1:65-76, 1996.
    • (1996) Folding Design , vol.1 , pp. 65-76
    • Barbar, E.1    Barany, G.2    Woodward, C.3
  • 248
    • 0027057526 scopus 로고
    • A database of protein structure families with common folding motifs
    • Holm, L., Ouzounis, C., Sander, C., Tuparev, G., Vriend, G. A database of protein structure families with common folding motifs. Protein Sci. 1:1691-1698, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 1691-1698
    • Holm, L.1    Ouzounis, C.2    Sander, C.3    Tuparev, G.4    Vriend, G.5
  • 249
  • 250
    • 0028373667 scopus 로고
    • Structure-based identification and clustering of protein families and superfamilies
    • Rufino, C.D., Blundell, T.L. Structure-based identification and clustering of protein families and superfamilies. J. Comp. Aided Mol. Design 8:5-27, 1994.
    • (1994) J. Comp. Aided Mol. Design , vol.8 , pp. 5-27
    • Rufino, C.D.1    Blundell, T.L.2
  • 251
    • 0028961335 scopus 로고
    • SCOP: A structural classification of protein database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., Chothia, C. SCOP: A structural classification of protein database for the investigation of sequences and structures. J. Mol. Biol. 247:536-540, 1995.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 252
    • 0028319318 scopus 로고
    • Classification of protein folds
    • Orengo, C. Classification of protein folds. Curr. Opin. Struct. Biol. 4:429-440, 1994.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 429-440
    • Orengo, C.1
  • 253
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L., Sander, C. Mapping the protein universe. Science 273:595-602, 1996.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 254
    • 15844411672 scopus 로고    scopus 로고
    • Extending molecular systematics to the third dimension
    • Wodak, S.J. Extending molecular systematics to the third dimension. Nature Struct. Biol. 3:575-578, 1996.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 575-578
    • Wodak, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.