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Volumn 33, Issue 3, 1998, Pages 358-366

Sequence and structure conservation in a protein core

Author keywords

Homologous proteins; Protein evolution; Protein structure; Sequence conservation; Sequence structure relationships; Superfamilies

Indexed keywords

PROTEIN;

EID: 0032534026     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19981115)33:3<358::AID-PROT5>3.0.CO;2-0     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 0023305986 scopus 로고
    • Knowledge-based prediction of protein structure and the design of novel molecules
    • Blundell, T.L., Sibanda, B.L., Sternberg, M.J.E., Thornton, J.M. Knowledge-based prediction of protein structure and the design of novel molecules. Nature 326: 347-352, 1987.
    • (1987) Nature , vol.326 , pp. 347-352
    • Blundell, T.L.1    Sibanda, B.L.2    Sternberg, M.J.E.3    Thornton, J.M.4
  • 2
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu, T.T., Kabat, E.A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J. Exp. Med. 132:211-249, 1970.
    • (1970) J. Exp. Med. , vol.132 , pp. 211-249
    • Wu, T.T.1    Kabat, E.A.2
  • 3
    • 0026342532 scopus 로고
    • Information-theoretical entropy as a measure of sequence variability
    • Shenkin, P.S., Erman, B., Mastandrea, L.D. Information-theoretical entropy as a measure of sequence variability. Proteins 11:297-313, 1991.
    • (1991) Proteins , vol.11 , pp. 297-313
    • Shenkin, P.S.1    Erman, B.2    Mastandrea, L.D.3
  • 5
    • 0023645034 scopus 로고
    • Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins
    • Cornette, J.L., Cease, K.B., Margalit, H., Spouge, J.L., Berzofsky, J.A, DeLisi, C. Hydrophobicity scales and computational techniques for detecting amphipathic structures in proteins. J. Mol. Biol. 195:659-685, 1987.
    • (1987) J. Mol. Biol. , vol.195 , pp. 659-685
    • Cornette, J.L.1    Cease, K.B.2    Margalit, H.3    Spouge, J.L.4    Berzofsky, J.A.5    DeLisi, C.6
  • 6
    • 0022591495 scopus 로고
    • The classification of amino-acid conservation
    • Taylor, W.R. The classification of amino-acid conservation. J. Theor. Biol. 119:205-218, 1986.
    • (1986) J. Theor. Biol. , vol.119 , pp. 205-218
    • Taylor, W.R.1
  • 7
    • 0029922443 scopus 로고    scopus 로고
    • Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins
    • Tomii, K., Kanehisa, M. Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins. Protein Eng. 9:27-36, 1996.
    • (1996) Protein Eng. , vol.9 , pp. 27-36
    • Tomii, K.1    Kanehisa, M.2
  • 8
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Silver Spring, MD:National Biomedical Research Foundation
    • Dayhoff, M.O., Schwartz, R.M., Orcutt, B.C. A model of evolutionary change in proteins. In: "Atlas of Protein Sequence and Structure." Vol. 5, Suppl. 3, Silver Spring, MD:National Biomedical Research Foundation, 1978:345-352.
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.3 SUPPL. , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 9
    • 3643138684 scopus 로고
    • Applications of environment specific amino acid substitution tables to identification of key residues in protein tertiary structure
    • Overington, J.P, Johnson, M.S., Topham, C., McLeod, A., Sali, A., Zhu, Z.-Y., Sibanda, L, Blundell, T.L. Applications of environment specific amino acid substitution tables to identification of key residues in protein tertiary structure. Curr. Sci. 59:867-874, 1990.
    • (1990) Curr. Sci. , vol.59 , pp. 867-874
    • Overington, J.P.1    Johnson, M.S.2    Topham, C.3    McLeod, A.4    Sali, A.5    Zhu, Z.-Y.6    Sibanda, L.7    Blundell, T.L.8
  • 10
    • 0027293521 scopus 로고
    • Molecular recognition in protein families: A database of aligned three-dimensional structures of related proteins
    • Overington, J.P. Zhu, Z.-Y., Sali, A. et al. Molecular recognition in protein families: A database of aligned three-dimensional structures of related proteins. Biochem. Soc. Trans. 21:597-604, 1993.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 597-604
    • Overington, J.P.1    Zhu, Z.-Y.2    Sali, A.3
  • 11
    • 0027305858 scopus 로고
    • Alignment and searching for common protein fold using a data bank of structural templates
    • Johnson, M.S., Overington, J.P., Blundell, T.L. Alignment and searching for common protein fold using a data bank of structural templates. J. Mol. Biol. 231:735-752, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 735-752
    • Johnson, M.S.1    Overington, J.P.2    Blundell, T.L.3
  • 12
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., Lesk, A.M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:823-826, 1986.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 13
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation
    • Russell, R.B., Saqi, M.A., Bates, P.A., Sternberg, M.J. Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation. J. Mol. Biol. 269:423-439, 1997.
    • (1997) J. Mol. Biol. , vol.269 , pp. 423-439
    • Russell, R.B.1    Saqi, M.A.2    Bates, P.A.3    Sternberg, M.J.4
  • 14
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., Chothia, C. SCOP: a structural classification of proteins 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
  • 15
    • 0030348027 scopus 로고    scopus 로고
    • A database of globular protein structural domains: Clustering of representative family members into similar folds
    • Sowdhamini, R., Rufino, S.D., Blundell, T.L. A database of globular protein structural domains: Clustering of representative family members into similar folds. Folding & Design, 1:209-220, 1996.
    • (1996) Folding & Design , vol.1 , pp. 209-220
    • Sowdhamini, R.1    Rufino, S.D.2    Blundell, T.L.3
  • 16
    • 0028274954 scopus 로고
    • Intramolecular cavities in globular proteins
    • Hubbard, S.J., Gross, K.H., Argos, P. Intramolecular cavities in globular proteins. Protein Eng. 7:613-626, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 613-626
    • Hubbard, S.J.1    Gross, K.H.2    Argos, P.3
  • 17
    • 0025269891 scopus 로고
    • Novel method for the rapid evaluation of packing in protein structure
    • Gregoret, L.M., Cohen, F.E. Novel method for the rapid evaluation of packing in protein structure. J. Mol. Biol. 211:959-974, 1990.
    • (1990) J. Mol. Biol. , vol.211 , pp. 959-974
    • Gregoret, L.M.1    Cohen, F.E.2
  • 18
    • 0038180490 scopus 로고
    • The analysis of protein three-dimensional structures in terms of residue-residue contact matrices. II. Coordination numbers
    • Rodionov, M.A., Galaktionov, S.G. The analysis of protein three-dimensional structures in terms of residue-residue contact matrices. II. Coordination numbers. Mol. Biol. 26:777-783, 1992.
    • (1992) Mol. Biol. , vol.26 , pp. 777-783
    • Rodionov, M.A.1    Galaktionov, S.G.2
  • 19
    • 0028247378 scopus 로고
    • Measuring residue association in protein structures
    • Karlin, S., Zuker, M., Brocchieri, L. Measuring residue association in protein structures. J. Mol. Biol. 239:227-248, 1994.
    • (1994) J. Mol. Biol. , vol.239 , pp. 227-248
    • Karlin, S.1    Zuker, M.2    Brocchieri, L.3
  • 20
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favourable contact pair term and unfavourable high packing density term, for simulation and threading
    • Miyazawa, S., Jernigan, R.L. Residue-residue potentials with a favourable contact pair term and unfavourable high packing density term, for simulation and threading. J. Mol. Biol. 256:623-644, 1996.
    • (1996) J. Mol. Biol. , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 21
    • 0001433241 scopus 로고
    • Knowledge based modelling of homologous proteins. Part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures
    • Sutcliffe, M.J., Haneef, I., Carney, D., Blundell, T.L. Knowledge based modelling of homologous proteins. Part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures. Protein Eng. 1:377-384, 1987.
    • (1987) Protein Eng. , vol.1 , pp. 377-384
    • Sutcliffe, M.J.1    Haneef, I.2    Carney, D.3    Blundell, T.L.4
  • 22
    • 0027136282 scopus 로고
    • Comparative modelling by satisfaction of spatial restraints
    • Sali, A., Blundell, T.L. Comparative modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815, 1993.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 23
    • 20544433165 scopus 로고
    • Van der Waals volumes and radii
    • Bondi, A. Van der Waals volumes and radii. J. Phys. Chem. 68:441-447, 1964.
    • (1964) J. Phys. Chem. , vol.68 , pp. 441-447
    • Bondi, A.1
  • 24
    • 0021118489 scopus 로고
    • Evolution and the tertiary structure of proteins
    • Bajaj, M., Blundell, T.L. Evolution and the tertiary structure of proteins. Annu. Rev. Biophys. Bioeng. 13:453-492, 1984.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 453-492
    • Bajaj, M.1    Blundell, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.