메뉴 건너뛰기




Volumn 4, Issue 10, 1996, Pages 1123-1127

A structural explanation for the twilight zone of protein sequence homology

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0009130599     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00119-0     Document Type: Article
Times cited : (114)

References (26)
  • 2
    • 0000840656 scopus 로고
    • Structural similarity of DNA-binding domains of bacteriophage repressors and the globin core
    • Subbiah, S., Laurents, D. & Levitt, M. (1993). Structural similarity of DNA-binding domains of bacteriophage repressors and the globin core. Curr. Biol. 3, 141-148.
    • (1993) Curr. Biol. , vol.3 , pp. 141-148
    • Subbiah, S.1    Laurents, D.2    Levitt, M.3
  • 3
    • 0028579713 scopus 로고
    • Different protein sequences can give rise to highly similar folds through different stabilizing interactions
    • Laurents, D., Subbiah, S. & Levitt, M. (1994). Different protein sequences can give rise to highly similar folds through different stabilizing interactions. Protein Sci. 3, 1938-1944.
    • (1994) Protein Sci. , vol.3 , pp. 1938-1944
    • Laurents, D.1    Subbiah, S.2    Levitt, M.3
  • 4
    • 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 9, 56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 5
    • 0019858614 scopus 로고
    • Similar amino acid sequences: Chance or common ancestry?
    • Doolittle, R.F. (1981). Similar amino acid sequences: chance or common ancestry? Science 214, 149-159.
    • (1981) Science , vol.214 , pp. 149-159
    • Doolittle, R.F.1
  • 6
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • Lesk, A.M. & Chothia, C. (1980). How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol. 136, 225-270.
    • (1980) J. Mol. Biol. , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 7
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C. & Lesk, A.M. (1986). The relation between the divergence of sequence and structure in proteins. EMBO J. 5, 823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 8
    • 12644250186 scopus 로고
    • Comparison of conformational characteristics in structurally similar protein pairs
    • Flores, T.P., Orengo, C.A., Moss, D.S., & Thornton, J.M. (1993). Comparison of conformational characteristics in structurally similar protein pairs. Protein Sci. 3, 2358-2365.
    • (1993) Protein Sci. , vol.3 , pp. 2358-2365
    • Flores, T.P.1    Orengo, C.A.2    Moss, D.S.3    Thornton, J.M.4
  • 9
    • 0030310218 scopus 로고    scopus 로고
    • How similar must a template protein be for homology modeling by side-chain packing methods
    • Hunter, L., & Klein, T., eds, Hawaii, USA
    • Chung, S.Y. & Subbiah, S. (1996). How similar must a template protein be for homology modeling by side-chain packing methods. In Proceedings of the first Pacific Symposium on Biocomputing. (Hunter, L., & Klein, T., eds), pp. 126-141, Hawaii, USA.
    • (1996) Proceedings of the First Pacific Symposium on Biocomputing , pp. 126-141
    • Chung, S.Y.1    Subbiah, S.2
  • 10
    • 0023155210 scopus 로고
    • Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder, J.W. & Richards, F.M. (1987). Tertiary templates for proteins: use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 11
    • 0026019108 scopus 로고
    • Prediction of protein side-chain conformation by packing optimization
    • Lee, C. & Subbiah, S.J. (1991). Prediction of protein side-chain conformation by packing optimization. Mol. Biol. 217, 373-388.
    • (1991) Mol. Biol. , vol.217 , pp. 373-388
    • Lee, C.1    Subbiah, S.J.2
  • 12
    • 0025978283 scopus 로고
    • Database algorithm for generating protein backbone and side-chain coordinates from a Cα trace application to model building and detection of coordinate errors
    • Holm, L. & Sander, C.J. (1991). Database algorithm for generating protein backbone and side-chain coordinates from a Cα trace application to model building and detection of coordinate errors. Mol. Biol. 218, 183-194.
    • (1991) Mol. Biol. , vol.218 , pp. 183-194
    • Holm, L.1    Sander, C.J.2
  • 13
    • 0026179489 scopus 로고
    • A new approach to the rapid determination of protein side chain conformations
    • Tuffery, P., Etchebest, C., Hazout, S. & Lavery, R.J. (1991). A new approach to the rapid determination of protein side chain conformations. Biomolec. Struct. Dyn. 8, 1267-1289.
    • (1991) Biomolec. Struct. Dyn. , vol.8 , pp. 1267-1289
    • Tuffery, P.1    Etchebest, C.2    Hazout, S.3    Lavery, R.J.4
  • 14
    • 0026589733 scopus 로고
    • The deadend elimination theorem and its use in protein side-chain prediction
    • Desmet, J., De Maeyer, M., Hazes, B., & Lasters, I. (1992). The deadend elimination theorem and its use in protein side-chain prediction. Nature 356, 539-542.
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    De Maeyer, M.2    Hazes, B.3    Lasters, I.4
  • 15
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins: Application to side-chain prediction
    • Dunbrack Jr., R.L. & Karplus, M.J. (1993).Backbone-dependent rotamer library for proteins: application to side-chain prediction. Mol. Biol. 230, 543-574.
    • (1993) Mol. Biol. , vol.230 , pp. 543-574
    • Dunbrack Jr., R.L.1    Karplus, M.J.2
  • 16
    • 0027185404 scopus 로고
    • A method to configure protein side-chain from the main-chain trace in homology modeling
    • Eisenmenger, F., Argos, P. & Abagyan, R. J. (1993). A method to configure protein side-chain from the main-chain trace in homology modeling. Mol. Biol. 231, 849-860.
    • (1993) Mol. Biol. , vol.231 , pp. 849-860
    • Eisenmenger, F.1    Argos, P.2    Abagyan, R.J.3
  • 17
    • 0027480460 scopus 로고
    • Modeling side-chain conformation for homologous proteins using an energy-based rotamer search
    • Wilson, C., Gregoret, L.M. & Agard, DA (1993). Modeling side-chain conformation for homologous proteins using an energy-based rotamer search. J. Mol. Biol. 229, 996-1006.
    • (1993) J. Mol. Biol. , vol.229 , pp. 996-1006
    • Wilson, C.1    Gregoret, L.M.2    Agard, D.A.3
  • 18
    • 0028343413 scopus 로고
    • Application of a self-consistent mean field theory to predict protein side-chain conformation and estimate their conformational energy
    • Koehl, P. & Delarue, M.J. (1994). Application of a self-consistent mean field theory to predict protein side-chain conformation and estimate their conformational energy. Mol. Biol. 239, 249-275.
    • (1994) Mol. Biol. , vol.239 , pp. 249-275
    • Koehl, P.1    Delarue, M.J.2
  • 19
    • 0028223845 scopus 로고
    • Prediction of protein mutant energetics by self-consistent ensemble optimization
    • Lee, C.J. (1994). Prediction of protein mutant energetics by self-consistent ensemble optimization. Mol. Biol. 236, 918-939.
    • (1994) Mol. Biol. , vol.236 , pp. 918-939
    • Lee, C.J.1
  • 20
    • 0028598623 scopus 로고
    • Prediction of protein mutant energetics by self-consistent ensemble optimization
    • Tanimura, R., Kidera, A. & Nakamura, H. (1994). Prediction of protein mutant energetics by self-consistent ensemble optimization. Protein Sci. 3, 2358-2365.
    • (1994) Protein Sci. , vol.3 , pp. 2358-2365
    • Tanimura, R.1    Kidera, A.2    Nakamura, H.3
  • 21
    • 0028786978 scopus 로고
    • The use of side-chain packing methods in modeling bacteriophage repressor and cro proteins
    • Chung, S.Y. & Subbiah S. (1995). The use of side-chain packing methods in modeling bacteriophage repressor and cro proteins. Protein Sci. 4, 2300-2309.
    • (1995) Protein Sci. , vol.4 , pp. 2300-2309
    • Chung, S.Y.1    Subbiah, S.2
  • 23
    • 0028081403 scopus 로고
    • Structural features can be unconserved in proteins with similar folds
    • Russell, R.B. & Barton, G.J. (1994). Structural features can be unconserved in proteins with similar folds. J. Mol. Biol. 244, 332-350.
    • (1994) J. Mol. Biol. , vol.244 , pp. 332-350
    • Russell, R.B.1    Barton, G.J.2
  • 24
    • 0016606973 scopus 로고
    • Structural invariants in protein folding
    • Chothia, C. (1975). Structural invariants in protein folding. Nature 245, 304-308.
    • (1975) Nature , vol.245 , pp. 304-308
    • Chothia, C.1
  • 25
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton, T.E., ed., Freeman, NY, USA
    • Ptitsyn, O. (1992). The molten globule state. In Protein Folding. (Creighton, T.E., ed.), pp. 243-300, Freeman, NY, USA.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.1
  • 26
    • 0026694167 scopus 로고
    • A model of the molten globule state from molecular dynamics simulations
    • Daggett, V. & Levitt. M. (1992). A model of the molten globule state from molecular dynamics simulations. Proc. Natl. Acad. Sci. USA 89, 5142-5146.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5142-5146
    • Daggett, V.1    Levitt, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.