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Volumn 285, Issue 5, 1999, Pages 2177-2198

The atomic structure of protein-protein recognition sites

Author keywords

Conformation changes; Interface area; Packing density; Polar interactions; Protein protein complexes

Indexed keywords

PROTEINASE INHIBITOR; SOLVENT;

EID: 0003187567     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2439     Document Type: Article
Times cited : (1810)

References (121)
  • 1
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos P. An investigation of protein subunit and domain interfaces. Protein Eng. 2:1988;101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 6
    • 0028138403 scopus 로고
    • Roles of lipid modifications of transducin subunits in their GDP-dependent association and membrane binding
    • Bigay J., Faurobert E., Franco M., Chabre M. Roles of lipid modifications of transducin subunits in their GDP-dependent association and membrane binding. Biochemistry. 33:1994;14081-14090.
    • (1994) Biochemistry , vol.33 , pp. 14081-14090
    • Bigay, J.1    Faurobert, E.2    Franco, M.3    Chabre, M.4
  • 7
    • 0027412820 scopus 로고
    • Binding of aminoacid side chains to preformed cavities: Interaction of serine proteases with turkey ovomucoid third domains with coded and noncoded P1 residues
    • Bigler T. L., Lu W., Park S. J., Tashiro M., Wieczorek M., Wynn R., Laskowski M. Jr. Binding of aminoacid side chains to preformed cavities: interaction of serine proteases with turkey ovomucoid third domains with coded and noncoded P1 residues. Protein Sci. 2:1993;786-799.
    • (1993) Protein Sci. , vol.2 , pp. 786-799
    • Bigler, T.L.1    Lu, W.2    Park, S.J.3    Tashiro, M.4    Wieczorek, M.5    Wynn, R.6    Laskowski M., Jr.7
  • 8
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding
    • Bode W., Schwager P., Huber R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. J. Mol. Biol. 118:1978;99-112.
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 9
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human leukocyte (Pmn elastase) and the third domain of the turkey ovomucoid inhibitor
    • Bode W., Wei A. Z., Huber R., Meyer E., Travis J., Neumann S. X-ray crystal structure of the complex of human leukocyte (Pmn elastase) and the third domain of the turkey ovomucoid inhibitor. EMBO J. 5:1986;2453-2458.
    • (1986) EMBO J. , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 10
    • 0023643147 scopus 로고
    • The high resolution X-ray crystal structure of the complex formed between subtilsin Carlsberg and eglin C, an elastase inhibitor from the leech Hirudo medicinalis
    • Bode W., Papamokas E., Musil D. The high resolution X-ray crystal structure of the complex formed between subtilsin Carlsberg and eglin C, an elastase inhibitor from the leech Hirudo medicinalis. Eur. J. Biochem. 166:1987;673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokas, E.2    Musil, D.3
  • 11
    • 0032479179 scopus 로고    scopus 로고
    • An analysis of hot spots in protein interfaces
    • Bogan A. A., Thorn K. S. An analysis of hot spots in protein interfaces. J. Mol. Biol. 280:1998;1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 12
    • 0020491487 scopus 로고
    • Three-dimensional structure of the complex between pancreatic secretory inhibitor (Kazal type) and trypsinogen at 1.8 Å resolution
    • Bolognesi M., Gatti G., Menegatti E., Guarneri M., Marquart M., Papamokos E., Huber R. Three-dimensional structure of the complex between pancreatic secretory inhibitor (Kazal type) and trypsinogen at 1.8 Å resolution. J. Mol. Biol. 162:1982;839-868.
    • (1982) J. Mol. Biol. , vol.162 , pp. 839-868
    • Bolognesi, M.1    Gatti, G.2    Menegatti, E.3    Guarneri, M.4    Marquart, M.5    Papamokos, E.6    Huber, R.7
  • 13
    • 0030589635 scopus 로고    scopus 로고
    • Substrate mimicry in the active center of mammalian α-amylase: Structural analysis of an enzyme-inhibitor complex
    • Bompard-Gilles C., Rousseau P., Rougé P., Payan P. Substrate mimicry in the active center of mammalian α-amylase: structural analysis of an enzyme-inhibitor complex. Structure. 4:1996;1441-1452.
    • (1996) Structure , vol.4 , pp. 1441-1452
    • Bompard-Gilles, C.1    Rousseau, P.2    Rougé, P.3    Payan, P.4
  • 14
    • 0028828994 scopus 로고
    • The crystal structure of the antibody N10-Staphylococcal nuclease complex at 2.9 Å resolution
    • Bossart-Whitaker P., Chang C. Y., Novotny J., Benjamin D. C., Sheriff S. The crystal structure of the antibody N10-Staphylococcal nuclease complex at 2.9 Å resolution. J. Mol. Biol. 253:1995;559-575.
    • (1995) J. Mol. Biol. , vol.253 , pp. 559-575
    • Bossart-Whitaker, P.1    Chang, C.Y.2    Novotny, J.3    Benjamin, D.C.4    Sheriff, S.5
  • 15
    • 0027971497 scopus 로고
    • Three-dimensional structures of the free and antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1
    • Braden B. C., Souchon H., Eiselé J.-L., Bentley G. A., Bhat T. N., Navaza J. N., Poljak R. J. Three-dimensional structures of the free and antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1. J. Mol. Biol. 242:1994;767-781.
    • (1994) J. Mol. Biol. , vol.242 , pp. 767-781
    • Braden, B.C.1    Souchon, H.2    Eiselé, J.-L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.N.6    Poljak, R.J.7
  • 17
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structural analysis of a barnase-barstar complex at 2.0 Å resolution
    • Buckle A. M., Schreiber G., Fersht A. R. Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0 Å resolution. Biochemistry. 33:1994;8878-8889.
    • (1994) Biochemistry , vol.33 , pp. 8878-8889
    • Buckle, A.M.1    Schreiber, G.2    Fersht, A.R.3
  • 18
    • 0029766569 scopus 로고    scopus 로고
    • Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: Effects on the kinetics and thermodynamics of binding to β-trypsin and a-chymotrypsin
    • Castro M. J., Anderson S. Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: effects on the kinetics and thermodynamics of binding to β-trypsin and a-chymotrypsin. Biochemistry. 35:1996;11435-11446.
    • (1996) Biochemistry , vol.35 , pp. 11435-11446
    • Castro, M.J.1    Anderson, S.2
  • 19
    • 0020645978 scopus 로고
    • Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor
    • Chen Z., Bode W. Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. J. Mol. Biol. 164:1983;283-311.
    • (1983) J. Mol. Biol. , vol.164 , pp. 283-311
    • Chen, Z.1    Bode, W.2
  • 21
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia C. Structural invariants in protein folding. Nature. 254:1975;304-308.
    • (1975) Nature , vol.254 , pp. 304-308
    • Chothia, C.1
  • 22
    • 0344329218 scopus 로고    scopus 로고
    • Protein-protein and protein-carbohydrate recognition
    • M. A. McCrae, J. R. Saunders, C. J. Smyth, & N. D. Stow. Cambridge University Press
    • Chothia C. Protein-protein and protein-carbohydrate recognition. McCrae M. A., Saunders J. R., Smyth C. J., Stow N. D. Molecular Aspects of Host-Pathogen Interaction. 1997;Cambridge University Press.
    • (1997) Molecular Aspects of Host-Pathogen Interaction
    • Chothia, C.1
  • 23
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia C., Janin J. Principles of protein-protein recognition. Nature. 256:1975;705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 24
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J. A. A hot spot of binding energy in a hormone-receptor interface. Science. 267:1995;383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 25
    • 0027132013 scopus 로고
    • Comparison of a structural and functional epitope
    • Cunningham B. C., Wells J. A. Comparison of a structural and functional epitope. J. Mol. Biol. 234:1993;554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 26
    • 0029764534 scopus 로고    scopus 로고
    • A mutational analysis of bthe inding of two different proteins to the same antibody
    • Dall'Acqua W., Goldman E. R., Eisenstein E., Mariuzza R. A. A mutational analysis of bthe inding of two different proteins to the same antibody. Biochemistry. 35:1996;9667-9676.
    • (1996) Biochemistry , vol.35 , pp. 9667-9676
    • Dall'Acqua, W.1    Goldman, E.R.2    Eisenstein, E.3    Mariuzza, R.A.4
  • 28
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D. R., Cohen G. H. Interactions of protein antigens with antibodies. Proc. Natl Acad. Sci. USA. 93:1996;7-12.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 29
    • 0019522383 scopus 로고
    • Crystallographic refinement and atonic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureus at 2.9 and 2.8 Å resolution
    • Deisenhofer J. Crystallographic refinement and atonic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureus at 2.9 and 2.8 Å resolution. Biochemistry. 20:1981;2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 30
    • 0028080176 scopus 로고
    • The third IgG-binding domain from streptococcal protein G
    • Derrick J. P., Wigley D. B. The third IgG-binding domain from streptococcal protein G. J. Mol. Biol. 243:1994;906-918.
    • (1994) J. Mol. Biol. , vol.243 , pp. 906-918
    • Derrick, J.P.1    Wigley, D.B.2
  • 32
    • 0029860018 scopus 로고    scopus 로고
    • Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitor H7, H8 and H89. Structural implications for selectivity
    • Engh R. A., Girod A., Kinzel V., Huber R., Bossemeyer D. Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitor H7, H8 and H89. Structural implications for selectivity. J. Biol. Chem. 271:1996;26157-26164.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26157-26164
    • Engh, R.A.1    Girod, A.2    Kinzel, V.3    Huber, R.4    Bossemeyer, D.5
  • 34
    • 0023198896 scopus 로고
    • Crystal and molecular structures of α-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution
    • Fujinaga M., Sielecki R., Read R. J., Ardelt W., Laskowski M., James M. N. J. Crystal and molecular structures of α-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution. J. Mol. Biol. 195:1987;397-418.
    • (1987) J. Mol. Biol. , vol.195 , pp. 397-418
    • Fujinaga, M.1    Sielecki, R.2    Read, R.J.3    Ardelt, W.4    Laskowski, M.5    James, M.N.J.6
  • 36
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi D. N., Ghosh P., Utz U., Fan Q. R., Biddison W. E., Wiley D. C. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature. 384:1996;134-141.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 37
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin
    • Gaudet R., Bohm A., Sigler P. B. Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin. Cell. 87:1996;577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 38
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface calculated from simulation using Voronoi polyhedra
    • Gerstein M., Tsai J., Levitt M. The volume of atoms on the protein surface calculated from simulation using Voronoi polyhedra. J. Mol. Biol. 249:1995;955-966.
    • (1995) J. Mol. Biol. , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3
  • 39
    • 0031021982 scopus 로고    scopus 로고
    • Analysis of binding interactions in an idiotope-antiidiotope protein-protein complex by double mutant cycles
    • Goldman E. R., Dall'Acqua W., Braden B. C., Mariuzza R. A. Analysis of binding interactions in an idiotope-antiidiotope protein-protein complex by double mutant cycles. Biochemistry. 36:1997;49-56.
    • (1997) Biochemistry , vol.36 , pp. 49-56
    • Goldman, E.R.1    Dall'Acqua, W.2    Braden, B.C.3    Mariuzza, R.A.4
  • 40
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S., Pavletich N. P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science. 274:1996;1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 42
    • 0027132431 scopus 로고
    • Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar
    • Guillet V., Lapthorn A., Hartley R. W., Mauguen Y. Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar. Structure. 1:1993;165-177.
    • (1993) Structure , vol.1 , pp. 165-177
    • Guillet, V.1    Lapthorn, A.2    Hartley, R.W.3    Mauguen, Y.4
  • 43
    • 0029646114 scopus 로고
    • Crystal structure of an acetylcholinesterase-fasciclin complex: Interaction of a three-fingered toxin from snake venom with its target
    • Harel M., Kleywegt G. J., Ravelli R. B. G., Silman I., Sussman J. L. Crystal structure of an acetylcholinesterase-fasciclin complex: interaction of a three-fingered toxin from snake venom with its target. Structure. 3:1995;1355-1366.
    • (1995) Structure , vol.3 , pp. 1355-1366
    • Harel, M.1    Kleywegt, G.J.2    Ravelli, R.B.G.3    Silman, I.4    Sussman, J.L.5
  • 44
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison C. J., Hayer-Hartl M., Di Liberto M., Hartl F. U., Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 276:1997;431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.U.4    Kuriyan, J.5
  • 45
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Harpaz Y., Gerstein M., Chothia C. Volume changes on protein folding. Structure. 2:1994;641-649.
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3
  • 46
    • 0030855425 scopus 로고    scopus 로고
    • The three-dimensional structure of a T-cell antigen receptor Vα-Vβ heterodimer reveals a novel rearrangement of the Vβ domain
    • Housset D., Mazza G., Grégoire C., Piras C., Malissen B., Fontecilla-Camps J. C. The three-dimensional structure of a T-cell antigen receptor Vα-Vβ heterodimer reveals a novel rearrangement of the Vβ domain. EMBO J. 16:1997;4205-4216.
    • (1997) EMBO J. , vol.16 , pp. 4205-4216
    • Housset, D.1    Mazza, G.2    Grégoire, C.3    Piras, C.4    Malissen, B.5    Fontecilla-Camps, J.C.6
  • 47
    • 0027516857 scopus 로고
    • The refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family
    • Huang Q., Liu S., Tang Y. The refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and MCTI-A, a trypsin inhibitor of the squash family. J. Mol. Biol. 229:1993;1022-1036.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1022-1036
    • Huang, Q.1    Liu, S.2    Tang, Y.3
  • 48
    • 0028856716 scopus 로고
    • Water molecules participate in protease-inhibitor interactions: Crystal structures of Leu-18, Ala-18 and Gly-18 variants of turkey ovomucoid inhibitor third domain in complex with S. griseus proteinase B
    • Huang K., Lu W., Anderson S., Laskowski M. Jr, James M. N. G. Water molecules participate in protease-inhibitor interactions: crystal structures of Leu-18, Ala-18 and Gly-18 variants of turkey ovomucoid inhibitor third domain in complex with S. griseus proteinase B. Protein Sci. 4:1995;1985-1997.
    • (1995) Protein Sci , vol.4 , pp. 1985-1997
    • Huang, K.1    Lu, W.2    Anderson, S.3    Laskowski M., Jr.4    James, M.N.G.5
  • 49
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II Crystallographic refinement at 1.9 Å resolution
    • Huber R., Kukla D., Bode W., Schwager P., Bartels K., Deisenhofer J., Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II Crystallographic refinement at 1.9 Å resolution. J. Mol. Biol. 89:1974;73-101.
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Deisenhofer, J.6    Steigemann, W.7
  • 51
    • 0028853544 scopus 로고
    • Principles of protein-protein recognition from structure to thermodynamics
    • Janin J. Principles of protein-protein recognition from structure to thermodynamics. Biochimie. 77:1995;497-505.
    • (1995) Biochimie , vol.77 , pp. 497-505
    • Janin, J.1
  • 52
    • 0029421048 scopus 로고    scopus 로고
    • Protein-protein recognition
    • Janin J. Protein-protein recognition. Prog. Biophys. Mol. Biol. 64:1996;145-165.
    • (1996) Prog. Biophys. Mol. Biol. , vol.64 , pp. 145-165
    • Janin, J.1
  • 53
    • 0017257628 scopus 로고
    • Stability and specificity of protein-protein interactions: The case of the trypsin-trypsin inhibitor complexes
    • Janin J., Chothia C. Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes. J. Mol. Biol. 100:1976;197-211.
    • (1976) J. Mol. Biol. , vol.100 , pp. 197-211
    • Janin, J.1    Chothia, C.2
  • 54
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J., Chothia C. The structure of protein-protein recognition sites. J. Biol. Chem. 265:1990;16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 55
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin J., Miller S., Chothia C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204:1988;155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 58
    • 0029109468 scopus 로고
    • Protein-protein interaction: A review of protein dimer structures
    • Jones S., Thornton J. M. Protein-protein interaction: a review of protein dimer structures. Prog. Biophys. Mol. Biol. 63:1995;131-165.
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 131-165
    • Jones, S.1    Thornton, J.M.2
  • 59
  • 60
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones S., Thornton J. M. Analysis of protein-protein interaction sites using surface patches. J. Mol. Biol. 272:1997;121-132.
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 62
  • 63
    • 0029093452 scopus 로고
    • Analysis of the factor VIIa binding site on human tissue factor: Effects of tissue factor mutations on the kinetics and thermodynamics of binding
    • Kelley R. F., Costas K. E., O'Connell M. P., Lazarus R. A. Analysis of the factor VIIa binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding. Biochemistry. 34:1995;10383-10392.
    • (1995) Biochemistry , vol.34 , pp. 10383-10392
    • Kelley, R.F.1    Costas, K.E.2    O'Connell, M.P.3    Lazarus, R.A.4
  • 64
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine rich repeats and protein ligands
    • Kobe B., Deisenhofer J. A structural basis of the interactions between leucine rich repeats and protein ligands. Nature. 374:1995;183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 65
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright D. G., Noel J. P., Hamm H. E., Sigler P. B. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature. 369:1994;621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 67
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence M. C., Colman P. M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234:1993;946-950.
    • (1993) J. Mol. Biol. , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 68
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F. M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 69
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved coreof HIV-1 nef complexed with a Src family SH3 domain
    • Lee C.-H., Saksela K., Mirza U. A., Chait B. T., Kuriyan J. Crystal structure of the conserved coreof HIV-1 nef complexed with a Src family SH3 domain. Cell. 85:1996;831-942.
    • (1996) Cell , vol.85 , pp. 831-942
    • Lee, C.-H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 71
    • 0030932886 scopus 로고    scopus 로고
    • Crystal structure of Lyme disease antigen OspA complexed with a Fab
    • Li H., Dunn J. J., Luft B. J., Lawson C. L. Crystal structure of Lyme disease antigen OspA complexed with a Fab. Proc. Natl Acad. Sci. USA. 94:1997;3584-3589.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3584-3589
    • Li, H.1    Dunn, J.J.2    Luft, B.J.3    Lawson, C.L.4
  • 73
    • 0028774037 scopus 로고
    • The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping site of the NC41 antibody
    • Malby R. L., Tulip W. R., Harley V. R., McKimm-Breschkin J. L., Laver W. G., Webster R. G., Colman P. M. The structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping site of the NC41 antibody. Structure. 2:1994;733-746.
    • (1994) Structure , vol.2 , pp. 733-746
    • Malby, R.L.1    Tulip, W.R.2    Harley, V.R.3    McKimm-Breschkin, J.L.4    Laver, W.G.5    Webster, R.G.6    Colman, P.M.7
  • 74
    • 0030802519 scopus 로고    scopus 로고
    • The co-crystal structure of unliganded bovine α-thrombin and prethrombin-2:movement of the Tyr-Pro-Pro-Trp segment upon ligand binding
    • Malkowski M. G., Martin P. D., Guzik G. C., Edwards B. F. The co-crystal structure of unliganded bovine α-thrombin and prethrombin-2:movement of the Tyr-Pro-Pro-Trp segment upon ligand binding. Protein Sci. 6:1997;1438-1448.
    • (1997) Protein Sci. , vol.6 , pp. 1438-1448
    • Malkowski, M.G.1    Martin, P.D.2    Guzik, G.C.3    Edwards, B.F.4
  • 75
    • 84977303841 scopus 로고
    • The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
    • Marquart M., Walter J., Deisenhofer J., Bode W., Huber R. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallog. sect. B. 39:1983;480-490.
    • (1983) Acta Crystallog. Sect. B , vol.39 , pp. 480-490
    • Marquart, M.1    Walter, J.2    Deisenhofer, J.3    Bode, W.4    Huber, R.5
  • 76
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I. K., Thornton J. M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:1994;777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 77
    • 0023729499 scopus 로고
    • Structural comparison of two serine proteinase-protein inhibitor complexes. Eglin C-subtilisin Carlsberg and CI 2-subtilisin novo
    • McPhalen C. A., James M. N. G. Structural comparison of two serine proteinase-protein inhibitor complexes. Eglin C-subtilisin Carlsberg and CI 2-subtilisin novo. Biochemistry. 27:1987;6582-6598.
    • (1987) Biochemistry , vol.27 , pp. 6582-6598
    • McPhalen, C.A.1    James, M.N.G.2
  • 79
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • Miller S., Lesk A. M., Janin J., Chothia C. The accessible surface area and stability of oligomeric proteins. Nature. 328:1987b;834-836.
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 81
    • 0029107760 scopus 로고    scopus 로고
    • The 2.2 Å crystal structure of the ras-binding domain of the serine/threonine kinase c-Raf1 in a complex with Rap1A and a GTP analogue
    • Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., Wittinghofer A. The 2.2 Å crystal structure of the ras-binding domain of the serine/threonine kinase c-Raf1 in a complex with Rap1A and a GTP analogue. Nature. 375:1996;554-660.
    • (1996) Nature , vol.375 , pp. 554-660
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 82
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1992;281-296.
    • (1992) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 83
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin complexes with GTPgS
    • Noel J. P., Hamm H. E., Sigler P. B. The 2.2 Å crystal structure of transducin complexes with GTPgS. Nature. 366:1993;654-662.
    • (1993) Nature , vol.366 , pp. 654-662
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 85
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochromec
    • Pelletier H., Kraut J. Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochromec. Science. 258:1992;1748-1755.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 87
    • 0021102433 scopus 로고
    • Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8 Å resolution
    • Read R. J., Fujinaga M., Sielecki R., James M. N. G. Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8 Å resolution. Biochemistry. 22:1983;4420-4433.
    • (1983) Biochemistry , vol.22 , pp. 4420-4433
    • Read, R.J.1    Fujinaga, M.2    Sielecki, R.3    James, M.N.G.4
  • 88
    • 0020491126 scopus 로고
    • Refined crystal structure of potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution
    • Rees D. C., Lipscomb W. N. Refined crystal structure of potato inhibitor complex of carboxypeptidase A at 2.5 Å resolution. J. Mol. Biol. 160:1982;475-498.
    • (1982) J. Mol. Biol. , vol.160 , pp. 475-498
    • Rees, D.C.1    Lipscomb, W.N.2
  • 89
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards F. M. The interpretation of protein structures: total volume, group volume distributions and packing density. J. Mol. Biol. 82:1974;1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 90
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase -activating protein in complex with a transition-state analogue
    • Rittinger K., Walker P. A., Eccleston J. F., Smerdon S. J., Gamblin S. J. Structure at 1.65 Å of RhoA and its GTPase -activating protein in complex with a transition-state analogue. Nature. 389:1997;758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 91
    • 0025866812 scopus 로고
    • The refined crystal structure of the hirudin-thrombin complex
    • Rydel T. J., Tulinsky A., Bode W., Huber R. The refined crystal structure of the hirudin-thrombin complex. J. Mol. Biol. 221:1991;583-601.
    • (1991) J. Mol. Biol. , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 92
    • 0029115366 scopus 로고
    • Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycoslase inhibitor protein complex
    • Savva R., Pearl L. H. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycoslase inhibitor protein complex. Nature Struct. Biol. 2:1995;752-757.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 752-757
    • Savva, R.1    Pearl, L.H.2
  • 93
    • 0030794907 scopus 로고    scopus 로고
    • Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid b-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI)
    • Scheidig A. J., Hynes T. R., Pelleyier L. A., Wells J. A., Kossiakoff A. A. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid b-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI). Protein Sci. 6:1997;1806-1824.
    • (1997) Protein Sci. , vol.6 , pp. 1806-1824
    • Scheidig, A.J.1    Hynes, T.R.2    Pelleyier, L.A.3    Wells, J.A.4    Kossiakoff, A.A.5
  • 94
    • 0027177102 scopus 로고
    • Interaction of barnase with its polypeptide inhibitor barstat studied by protein engineering
    • Schreiber G., Fersht A. R. Interaction of barnase with its polypeptide inhibitor barstat studied by protein engineering. Biochemistry. 32:1993;5145-5150.
    • (1993) Biochemistry , vol.32 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 95
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the Barnase-Barstar interface by single mutations and double mutant cycles
    • Schreiber G., Fersht A. R. Energetics of protein-protein interactions: analysis of the Barnase-Barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248:1995;478-486.
    • (1995) J. Mol. Biol. , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 99
    • 0032536108 scopus 로고    scopus 로고
    • Kunitz-type soybean trypsin inhibitor revisited: Refined structure of its complex with porcine trypsin reveals an insight of the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator
    • Song H. K., Suh S. W. Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight of the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. J. Mol. Biol. 275:1998;347-363.
    • (1998) J. Mol. Biol. , vol.275 , pp. 347-363
    • Song, H.K.1    Suh, S.W.2
  • 100
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran
    • Stewart M., Kent H. M., McCoy A. J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J. Mol. Biol. 277:1998;635-646.
    • (1998) J. Mol. Biol. , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 101
    • 0029949210 scopus 로고    scopus 로고
    • A potent new mode of β-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structute of the TEM-1-BLIP complex
    • Strynadka N. C. J., Jensen S. E., Alzari P. M., James M. N. G. A potent new mode of β-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structute of the TEM-1-BLIP complex. Nature Struct. Biol. 3:1996;290-297.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 290-297
    • Strynadka, N.C.J.1    Jensen, S.E.2    Alzari, P.M.3    James, M.N.G.4
  • 102
    • 0025301658 scopus 로고
    • The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinease papain: A novel type of proteinase inhibitor interaction
    • Stubbs M. T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V. The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinease papain: a novel type of proteinase inhibitor interaction. EMBO J. 9:1990;1939-1947.
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 103
    • 0029770041 scopus 로고    scopus 로고
    • Crystal structure of an antagonist mutant of human growth hormon G120R in complex with its receptor at 2.9 Å resolution
    • Sundström M., Lundqvist T., Rödin J., Giebel L. B., Milligan D., Norstedt G. Crystal structure of an antagonist mutant of human growth hormon G120R in complex with its receptor at 2.9 Å resolution. J. Biol. Chem. 271:1996;32197-32203.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32197-32203
    • Sundström, M.1    Lundqvist, T.2    Rödin, J.3    Giebel, L.B.4    Milligan, D.5    Norstedt, G.6
  • 104
    • 0025812630 scopus 로고
    • Refined crystal structure of the complex subtilisin BPN and Streptomyces subtilisin inhibitor at 1.8 Å resolution
    • Takeuchi Y., Satow Y., Nakamura K. T., Mitsui Y. Refined crystal structure of the complex subtilisin BPN and Streptomyces subtilisin inhibitor at 1.8 Å resolution. J. Mol. Biol. 221:1991;309-325.
    • (1991) J. Mol. Biol. , vol.221 , pp. 309-325
    • Takeuchi, Y.1    Satow, Y.2    Nakamura, K.T.3    Mitsui, Y.4
  • 106
    • 0030756203 scopus 로고    scopus 로고
    • Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and to protein-protein association
    • Tsai C. J., Nussinov R. Hydrophobic folding units at protein-protein interfaces: implications to protein folding and to protein-protein association. Protein Sci. 6:1997;1426-1437.
    • (1997) Protein Sci. , vol.6 , pp. 1426-1437
    • Tsai, C.J.1    Nussinov, R.2
  • 107
    • 0030602896 scopus 로고    scopus 로고
    • A dataset of protein-protein interfaces generated with a sequence order-independent comparison technique
    • Tsai J., Lin S. L., Wolfson H., Nussinov R. A dataset of protein-protein interfaces generated with a sequence order-independent comparison technique. J. Mol. Biol. 260:1996;604-620.
    • (1996) J. Mol. Biol. , vol.260 , pp. 604-620
    • Tsai, J.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 108
    • 0029811088 scopus 로고    scopus 로고
    • Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase
    • Tsunemi M., Matsuura Y., Sakakibara S., Katsube Y. Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase. Biochemistry. 35:1996;11570-11576.
    • (1996) Biochemistry , vol.35 , pp. 11570-11576
    • Tsunemi, M.1    Matsuura, Y.2    Sakakibara, S.3    Katsube, Y.4
  • 109
    • 0026781840 scopus 로고
    • Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex
    • Tulip W. R., Varghese J. N., Laver W. G., Webster R. G., Colman P. M. Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex. J. Mol. Biol. 227:1992;122-148.
    • (1992) J. Mol. Biol. , vol.227 , pp. 122-148
    • Tulip, W.R.1    Varghese, J.N.2    Laver, W.G.3    Webster, R.G.4    Colman, P.M.5
  • 110
    • 0028784163 scopus 로고
    • Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodnin in complex with thrombin
    • van de Locht A., Lamba D., Bauer M., Huber R., Friedrich T., Kröger B., Höffken W., Bode W. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodnin in complex with thrombin. EMBO J. 14:1995;5149-5157.
    • (1995) EMBO J. , vol.14 , pp. 5149-5157
    • Van De Locht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kröger, B.6    Höffken, W.7    Bode, W.8
  • 112
    • 0030959346 scopus 로고    scopus 로고
    • The thrombin E192Q-BPTI complex reveals gross structural rearrangements: Implications for the interaction with antithrombin and thrombomodulin
    • van de Locht A., Bode W., Huber R., Le Bonniec B. F., Stone S. R., Esmon C. T., Stubbs M. T. The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. EMBO J. 16:1997;2977-2984.
    • (1997) EMBO J. , vol.16 , pp. 2977-2984
    • Van De Locht, A.1    Bode, W.2    Huber, R.3    Le, B.B.F.4    Stone, S.R.5    Esmon, C.T.6    Stubbs, M.T.7
  • 113
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of thr complex
    • Vos A. M., de Ultsch M., Kossiakoff A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of thr complex. Science. 255:1992;306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • Vos, A.M.1    De Ultsch, M.2    Kossiakoff, A.A.3
  • 117
    • 0031975752 scopus 로고    scopus 로고
    • Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
    • Welch M., Chinardet N., Mourey L., Birck C., Samama J. P. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nature Struct. Biol. 5:1997;25-29.
    • (1997) Nature Struct. Biol , vol.5 , pp. 25-29
    • Welch, M.1    Chinardet, N.2    Mourey, L.3    Birck, C.4    Samama, J.P.5
  • 118
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells J. A. Binding in the growth hormone receptor complex. Proc. Natl Acad. Sci. USA. 93:1996;1-6.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 119
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D., Tsai C. J., Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng. 10:1997;999-1012.
    • (1997) Protein Eng. , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 120
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L., Jernigan R. L., Covell D. G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 3:1994;717-729.
    • (1994) Protein Sci. , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3


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