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Volumn 258, Issue 2, 1996, Pages 349-366

Structural diversity in a family of homologous proteins

Author keywords

Computer experiments; Protein families; Protein modeling; Protein structure analysis; Threading

Indexed keywords

CALCIUM BINDING PROTEIN;

EID: 0343961969     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0255     Document Type: Article
Times cited : (24)

References (42)
  • 1
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Angstroms resolution
    • Babu, Y. S., Bugg, C. E. & Cook, W. J. (1988). Structure of calmodulin refined at 2.2 Angstroms resolution. J. Mol. Biol. 204, 191.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 3
    • 0027373337 scopus 로고
    • Knowledge-based model building of proteins: Concepts and examples
    • Bajorath, J., Stenkamp, R. & Aruffo, A. (1993). Knowledge-based model building of proteins: concepts and examples. Protein Sci. 2, 1798-1810.
    • (1993) Protein Sci. , vol.2 , pp. 1798-1810
    • Bajorath, J.1    Stenkamp, R.2    Aruffo, A.3
  • 5
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three dimensional structure
    • Bowie, J. U., Luethy, R. & Eisenberg, D. (1991). A method to identify protein sequences that fold into a known three dimensional structure. Science, 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luethy, R.2    Eisenberg, D.3
  • 6
    • 0027318317 scopus 로고
    • An empirical energy function for threading protein sequence through folding motif
    • Bryant, S. H. & Lawrence, C. E. (1993). An empirical energy function for threading protein sequence through folding motif. Proteins: Struct. Funct Genet. 16, 92-112.
    • (1993) Proteins: Struct. Funct Genet. , vol.16 , pp. 92-112
    • Bryant, S.H.1    Lawrence, C.E.2
  • 7
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemmaglutinin
    • Carr, C. M. & Kim, P. S. (1993). A spring-loaded mechanism for the conformational change of influenza hemmaglutinin. Cell, 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 8
    • 0028054727 scopus 로고
    • Easy adaptation of protein structure to sequence
    • Chelvanayagam, G., Roy, G. & Argos, P. (1994). Easy adaptation of protein structure to sequence. Protein Eng. 7, 173-184.
    • (1994) Protein Eng. , vol.7 , pp. 173-184
    • Chelvanayagam, G.1    Roy, G.2    Argos, P.3
  • 9
    • 0027122748 scopus 로고
    • Proteins. One thousand families for the molecular biologist
    • Chothia, C. (1992). Proteins. One thousand families for the molecular biologist. Nature, 357, 543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 10
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure of proteins
    • Chothia, C. & Lesk, A. M. (1986). The relation between the divergence of sequence and structure of proteins. EMBO J. 5, 823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 11
    • 0023479421 scopus 로고
    • Why do globular proteins fit the limited set of folding patterns?
    • Finkelstein, A. V. & Ptitsyn, O. B. (1987). Why do globular proteins fit the limited set of folding patterns? Prog. Biophys. Mol. Biol. 50, 171-190.
    • (1987) Prog. Biophys. Mol. Biol. , vol.50 , pp. 171-190
    • Finkelstein, A.V.1    Ptitsyn, O.B.2
  • 12
    • 0025425518 scopus 로고
    • Determination of globular protein chain fold by the method of self-consistent field
    • Finkelstein, A. V. & Reva, B. A. (1990). Determination of globular protein chain fold by the method of self-consistent field (in Russian). Biofizika, 35, 402-406.
    • (1990) Biofizika , vol.35 , pp. 402-406
    • Finkelstein, A.V.1    Reva, B.A.2
  • 13
    • 0027429963 scopus 로고
    • Three-dimensional structure of recoverin, a calcium sensor in vision
    • Flaherty K. M. (1993). Three-dimensional structure of recoverin, a calcium sensor in vision. Cell Biol. 75, 706-716.
    • (1993) Cell Biol. , vol.75 , pp. 706-716
    • Flaherty K, M.1
  • 14
    • 0003648123 scopus 로고
    • April, 1991, 575 Science Drive, Madison, WI, 53711, USA
    • Genetic Computer Group (1991). Program Manual for the GCG Package, version 7, April, 1991, 575 Science Drive, Madison, WI, 53711, USA.
    • (1991) Program Manual for the GCG Package, Version 7
  • 15
    • 0342441707 scopus 로고
    • Sequence analysis of the troponin C superfamily
    • Godzik, A. & Boguta, G. (1989). Sequence analysis of the troponin C superfamily Studia Biophys. 129, 241-250.
    • (1989) Studia Biophys. , vol.129 , pp. 241-250
    • Godzik, A.1    Boguta, G.2
  • 16
    • 0026726481 scopus 로고
    • A topology fingerprint approach to the inverse folding problem
    • Godzik, A., Skolnick, J. & Kolinski, A. (1992). A topology fingerprint approach to the inverse folding problem. J. Mol. Biol. 227, 227-238.
    • (1992) J. Mol. Biol. , vol.227 , pp. 227-238
    • Godzik, A.1    Skolnick, J.2    Kolinski, A.3
  • 17
    • 0027504807 scopus 로고
    • Regularities in interaction patterns of globular proteins
    • Godzik, A., Skolnick, J. & Kolinski, A. (1993). Regularities in interaction patterns of globular proteins. Protein Eng. 6, 801-810.
    • (1993) Protein Eng. , vol.6 , pp. 801-810
    • Godzik, A.1    Skolnick, J.2    Kolinski, A.3
  • 18
    • 0028892389 scopus 로고
    • Are proteins ideal mixtures of amino acids? Analysis of energy parameter sets
    • Godzik, A., Kolinski, A. & Skolnick, J. (1995). Are proteins ideal mixtures of amino acids? Analysis of energy parameter sets. Protein Sci. 4, 2107-2117.
    • (1995) Protein Sci. , vol.4 , pp. 2107-2117
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 19
    • 0027363912 scopus 로고
    • Structural relationship of homologous proteins as a fundamental principle in homology modeling
    • Hilbert, M., Bohm, G. & Jaenicke, R. (1993). Structural relationship of homologous proteins as a fundamental principle in homology modeling. Proteins: Struct. Funct. Genet. 17, 138-151.
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 138-151
    • Hilbert, M.1    Bohm, G.2    Jaenicke, R.3
  • 20
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B. & Bax, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science, 256, 632.
    • (1992) Science , vol.256 , pp. 632
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 22
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones, D. T., Taylor, W. R. & Thornton, J. M. (1992). A new approach to protein fold recognition. Nature, 358, 86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 23
    • 0028678827 scopus 로고
    • Calcium binding proteins 1: EF-hands
    • Kawasaki, H. & Kretsinger, R. (1994). Calcium binding proteins 1: EF-hands. Protein Profile, 1, 343-517.
    • (1994) Protein Profile , vol.1 , pp. 343-517
    • Kawasaki, H.1    Kretsinger, R.2
  • 24
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 Å resolution of HIV-1 reverse trancriptase complexed with an inhibitor
    • Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A. & Steitz, T. A. (1992). Crystal structure at 3.5 Å resolution of HIV-1 reverse trancriptase complexed with an inhibitor. Science, 256, 1783.
    • (1992) Science , vol.256 , pp. 1783
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 25
    • 0018816959 scopus 로고
    • Structure and evolution of calcium modulated proteins
    • Kretsinger, R. H. (1980). Structure and evolution of calcium modulated proteins. CRC Crit. Rev. Biochem. 8, 119-174.
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 26
    • 0026610767 scopus 로고
    • Assesment of protein models with three dimensional profiles
    • Luethy R., Bowie, J. U. & Eisenberg, D. (1992). Assesment of protein models with three dimensional profiles. Nature, 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luethy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 27
    • 0026785519 scopus 로고
    • Contact potential that recognizes the correct folding of globular proteins
    • Maiorov, V. N. & Crippen, G. M. (1992). Contact potential that recognizes the correct folding of globular proteins. J. Mol. Biol. 277, 876-888.
    • (1992) J. Mol. Biol. , vol.277 , pp. 876-888
    • Maiorov, V.N.1    Crippen, G.M.2
  • 29
    • 0021691918 scopus 로고
    • An analysis of incorrectly folded protein models. Implications for structure prediction
    • Novotny J., Brucolleri, R. & Karplus, M. (1984). An analysis of incorrectly folded protein models. Implications for structure prediction. J. Mol. Biol. 177, 787-818.
    • (1984) J. Mol. Biol. , vol.177 , pp. 787-818
    • Novotny, J.1    Brucolleri, R.2    Karplus, M.3
  • 30
    • 0027302043 scopus 로고
    • Prediction of protein structure by evaluation of sequence-structure fitness: Aligning sequences to contact profiles derived from 3D structures
    • Ouzounis, C., Sander, C., Scharf, M. & Schneider, R. (1993). Prediction of protein structure by evaluation of sequence-structure fitness: aligning sequences to contact profiles derived from 3D structures. J. Mol. Biol. 232, 805-825.
    • (1993) J. Mol. Biol. , vol.232 , pp. 805-825
    • Ouzounis, C.1    Sander, C.2    Scharf, M.3    Schneider, R.4
  • 31
    • 0343311307 scopus 로고
    • June 1994
    • Protein Data Bank (1994). Quaterly Newsletter, no. 69, June 1994.
    • (1994) Quaterly Newsletter , vol.69
  • 35
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 36
    • 0025350388 scopus 로고
    • From comparison of protein sequences and structures to protein modelling and design
    • Sali, A., Overington, J. P., Johnson, M. S. & Blundell, T. L. (1990). From comparison of protein sequences and structures to protein modelling and design. Trends Biochem. Sci. 15, 235-240.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 235-240
    • Sali, A.1    Overington, J.P.2    Johnson, M.S.3    Blundell, T.L.4
  • 37
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander, C. & Schneider, R. (1991). Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins: Struct. Funct. Genet. 9, 56-68.
    • (1991) Proteins: Struct. Funct. Genet. , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 38
    • 0026704815 scopus 로고
    • Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a database of known protein conformations
    • Sippl, M. J. & Weitckus, S. (1992). Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a database of known protein conformations. Proteins: Struct Funct. Genet. 13, 258-271.
    • (1992) Proteins: Struct Funct. Genet. , vol.13 , pp. 258-271
    • Sippl, M.J.1    Weitckus, S.2
  • 39
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka, N. C. & James, M. N. (1989). Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58, 951-998.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 40
    • 0028038195 scopus 로고
    • Homology modelling of divergent proteins
    • S., S.
    • Sudarsanam, S., March, C. J. & S., S. (1994). Homology modelling of divergent proteins. J. Mol. Biol. 241, 143-149.
    • (1994) J. Mol. Biol. , vol.241 , pp. 143-149
    • Sudarsanam, S.1    March, C.J.2
  • 41
    • 0022972435 scopus 로고
    • The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine
    • Szebenyi, D. M. E. & Moffat, K. (1986). The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. J. Biol. Chem. 261, 8761.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8761
    • Szebenyi, D.M.E.1    Moffat, K.2
  • 42
    • 0026545366 scopus 로고
    • Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 Å resolution
    • Vijay-Kumar, S. & Cook, W. J. (1992). Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 Å resolution. J. Mol. Biol. 224, 413-426.
    • (1992) J. Mol. Biol. , vol.224 , pp. 413-426
    • Vijay-Kumar, S.1    Cook, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.