메뉴 건너뛰기




Volumn 15, Issue 7, 1996, Pages 675-690

Patterns and conformations of commonly occurring supersecondary structures (basic motifs) in protein data bank

Author keywords

basic motifs; Proten supersecondary structure; short connecting peptides; structure modeling

Indexed keywords

ARTICLE; DATA BASE; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0030461645     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01886750     Document Type: Article
Times cited : (25)

References (37)
  • 2
    • 0023305986 scopus 로고
    • Knowledge-based prediction of protein structures and the design of novel molecules
    • BLlundell, T. L., Sibanda, B. L., Sternberg, M. J. E., and Thronton, J. M. (1987). Knowledge-based prediction of protein structures and the design of novel molecules, Nature 323, 347-352.
    • (1987) Nature , vol.323 , pp. 347-352
    • Bllundell, T.L.1    Sibanda, B.L.2    Sternberg, M.J.E.3    Thronton, J.M.4
  • 4
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y., and Fasman, G. D. (1974). Prediction of protein conformation, Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 5
    • 0027461064 scopus 로고
    • Peptide conformation and protein folding
    • Dyson, H. J., and Wright, P. E. (1993). Peptide conformation and protein folding, Curr. Opin. Struct. Biol. 3, 60-65.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 60-65
    • Dyson, H.J.1    Wright, P.E.2
  • 6
    • 0342929492 scopus 로고
    • Structural and sequence patterns in the loops of βαβ units
    • Edwards, M. S., Sternberg, M. J., and Thornton, J. M. (1987). Structural and sequence patterns in the loops of βαβ units, Protein Eng. 1, 173-181.
    • (1987) Protein Eng. , vol.1 , pp. 173-181
    • Edwards, M.S.1    Sternberg, M.J.2    Thornton, J.M.3
  • 7
    • 0020360290 scopus 로고
    • Supersecondary structure of β-proteins
    • Efimov, A. V. (1982). Supersecondary structure of β-proteins, Mol. Biol. (Moscow) 16, 799-806.
    • (1982) Mol. Biol. (Moscow) , vol.16 , pp. 799-806
    • Efimov, A.V.1
  • 8
    • 0022565437 scopus 로고
    • Standard conformations of a poly-peptide chain in irregular regions of proteins
    • Efimov, A. V. (1986). Standard conformations of a poly-peptide chain in irregular regions of proteins, Mol. Biol. (Moscow) 20, 250-260.
    • (1986) Mol. Biol. (Moscow) , vol.20 , pp. 250-260
    • Efimov, A.V.1
  • 9
    • 0025974401 scopus 로고
    • Structure of β-β hairpin with short connections
    • Efimov, A. V. (1991). Structure of β-β hairpin with short connections, Protein Eng. 4, 245-250.
    • (1991) Protein Eng. , vol.4 , pp. 245-250
    • Efimov, A.V.1
  • 10
    • 0027284308 scopus 로고
    • Patterns of loop regions in proteins
    • Efimov, A. V. (1993). Patterns of loop regions in proteins, Curr. Opin. Struct. Biol. 3, 379-384.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 379-384
    • Efimov, A.V.1
  • 11
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted threedimensional solid model representations of macromolecules
    • Evans, S. V. (1993). SETOR: Hardware lighted threedimensional solid model representations of macromolecules, J. Mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 12
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein, J. (1985). Confidence limits on phylogenies: An approach using the bootstrap, Evolution 39, 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 13
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine protease
    • Greer, J. (1990). Comparative modeling methods: Application to the family of the mammalian serine protease, Proteins Struct. Fund. Genet. 7, 317-337.
    • (1990) Proteins Struct. Fund. Genet. , vol.7 , pp. 317-337
    • Greer, J.1
  • 14
    • 0029101826 scopus 로고
    • Recognizing native folds by the arrangement of hydrophobic and polar residues
    • Huang, E. S., Subbiah, S., and Levitt, M. (1995). Recognizing native folds by the arrangement of hydrophobic and polar residues, J. Mol. Biol. 252, 709-720.
    • (1995) J. Mol. Biol. , vol.252 , pp. 709-720
    • Huang, E.S.1    Subbiah, S.2    Levitt, M.3
  • 15
    • 0000338489 scopus 로고
    • Comparison of the solvent-inaccessible cores of homologous proteins: Definitions useful for protein modeling
    • Hubbard, T. J. P., and Blundell, T. L. (1987). Comparison of the solvent-inaccessible cores of homologous proteins: Definitions useful for protein modeling, Protein Eng. 1, 159-171.
    • (1987) Protein Eng. , vol.1 , pp. 159-171
    • Hubbard, T.J.P.1    Blundell, T.L.2
  • 16
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones, T. H., and Thirup, S. (1986). Using known substructures in protein model building and crystallography, EMBO J. 5, 819-822..
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.H.1    Thirup, S.2
  • 17
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 18
    • 0016209912 scopus 로고
    • Structural principles of globular organization of protein chains, A stereochemical theory of globular protein secondary structure
    • Lim, V. I. (1974). Structural principles of globular organization of protein chains, A stereochemical theory of globular protein secondary structure, J. Mol. Biol. 88, 857-872.
    • (1974) J. Mol. Biol. , vol.88 , pp. 857-872
    • Lim, V.I.1
  • 19
    • 0000243829 scopus 로고
    • Computer program-PROCHECK: A program to check the seterochemical quality of protein structure
    • MacArthus, M. W., Laskowski, R. A., Moss, D. S., and Thornton, J. M. (1993). Computer program-PROCHECK: A program to check the seterochemical quality of protein structure, J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • MacArthus, M.W.1    Laskowski, R.A.2    Moss, D.S.3    Thornton, J.M.4
  • 20
    • 0026655361 scopus 로고
    • Stereochemical quality of protein structure coordinates
    • Morris, A. L., MacArthur, M. W., Hutchinson, E. G., Thornton, J. M., et al. (1992). Stereochemical quality of protein structure coordinates, Proteins, 12, 345-364.
    • (1992) Proteins , vol.12 , pp. 345-364
    • Morris, A.L.1    MacArthur, M.W.2    Hutchinson, E.G.3    Thornton, J.M.4
  • 21
    • 0027062943 scopus 로고
    • Environment-specific amino acid substitution tables: Tertiary templates and prediction of protein fold
    • Overington, J., Donnelly, D., Johnson, M. S., Sali, A., and Blundell, T. L. (1992). Environment-specific amino acid substitution tables: Tertiary templates and prediction of protein fold, Protein Sci. 1, 216-226.
    • (1992) Protein Sci. , vol.1 , pp. 216-226
    • Overington, J.1    Donnelly, D.2    Johnson, M.S.3    Sali, A.4    Blundell, T.L.5
  • 22
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981). The anatomy and taxonomy of protein structure, Adv. Protein Chem. 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 23
    • 0017876485 scopus 로고
    • Packing of α-helices: Geometrical constraints and contact areas
    • Richmond, T. J., and Richards, F. M. (1978). Packing of α-helices: Geometrical constraints and contact areas, J. Mol. Biol. 119, 537-555.
    • (1978) J. Mol. Biol. , vol.119 , pp. 537-555
    • Richmond, T.J.1    Richards, F.M.2
  • 24
    • 0025326949 scopus 로고
    • Automatic definition of recurrent local structure motif in proteins
    • Rooman, M. J., Rodriguez, J., and Wodak, S. J. (1990). Automatic definition of recurrent local structure motif in proteins, J. Mol. Biol. 213, 327-336.
    • (1990) J. Mol. Biol. , vol.213 , pp. 327-336
    • Rooman, M.J.1    Rodriguez, J.2    Wodak, S.J.3
  • 25
    • 0025317502 scopus 로고
    • Definition of general topological equivalence in protein structures
    • Sali, A., and Blundell, T. L. (1990). Definition of general topological equivalence in protein structures, J. Mol. Biol. 212, 403-428.
    • (1990) J. Mol. Biol. , vol.212 , pp. 403-428
    • Sali, A.1    Blundell, T.L.2
  • 26
    • 0026773958 scopus 로고
    • Recurrent αβ lops in TIM barrel motifs show a distinct pattern of conserved structural feature Proteins Struct
    • Scheerlinck, J. P. Y., Lasters, I., Claessens, M., De Maeyer, M., Pio, F., Drlhaise, P., and Wodak, S. J. (1992). Recurrent αβ lops in TIM barrel motifs show a distinct pattern of conserved structural feature Proteins Struct. Fund. Genet. 12, 299-313.
    • (1992) Fund. Genet. , vol.12 , pp. 299-313
    • Scheerlinck, J.P.Y.1    Lasters, I.2    Claessens, M.3    De Maeyer, M.4    Pio, F.5    Drlhaise, P.6    Wodak, S.J.7
  • 27
    • 0021844602 scopus 로고
    • β-Hairpin families in globular proteins
    • Sibanda, B. L., and Thornton, J. M. (1985). β-Hairpin families in globular proteins, Nature 316, 170-174.
    • (1985) Nature , vol.316 , pp. 170-174
    • Sibanda, B.L.1    Thornton, J.M.2
  • 28
    • 0027339355 scopus 로고
    • Accommodating sequence changes in β-hairpins in proteins
    • Sibanda, B. L., and Thornton, J. M. (1993). Accommodating sequence changes in β-hairpins in proteins, J. Mol. Biol. 229, 428-447.
    • (1993) J. Mol. Biol. , vol.229 , pp. 428-447
    • Sibanda, B.L.1    Thornton, J.M.2
  • 29
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modeling by homology, electron density fitting and protein engineering
    • Sibanda, B. L., Blundell, T. L., and Thornton, J. M. (1989). Conformation of β-hairpins in protein structures. A systematic classification with applications to modeling by homology, electron density fitting and protein engineering, J. Mol. Biol. 206, 759-777.
    • (1989) J. Mol. Biol. , vol.206 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 30
    • 0001433241 scopus 로고
    • Knowledge based modelling of homologous proteins, Part I
    • Sutcliffe, M. J., Haneef, I., Carney, D., and Blundell, T. L. (1987). Knowledge based modelling of homologous proteins, Part I, Protein Eng. 1, 377-384.
    • (1987) Protein Eng. , vol.1 , pp. 377-384
    • Sutcliffe, M.J.1    Haneef, I.2    Carney, D.3    Blundell, T.L.4
  • 31
    • 0023955009 scopus 로고
    • Analysis, design, and modification of loop regions in proteins
    • Thornton, J. M., Sibanda, B. L., Edwanlo, M. S., and Barlow, D. J. (1988). Analysis, design, and modification of loop regions in proteins, Bioessays 8, 63-70.
    • (1988) Bioessays , vol.8 , pp. 63-70
    • Thornton, J.M.1    Sibanda, B.L.2    Edwanlo, M.S.3    Barlow, D.J.4
  • 34
    • 0027645984 scopus 로고
    • The importance of short structural motifs in protein structure analysis
    • Unger, R., and Sussman, J. L. (1993). The importance of short structural motifs in protein structure analysis, J. Comp. Aided Mol. Des. 7, 457-472.
    • (1993) J. Comp. Aided Mol. Des. , vol.7 , pp. 457-472
    • Unger, R.1    Sussman, J.L.2
  • 35
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • West, M., and Hecht, M. (1995). Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins, Protein Sci. 4, 2032-2039.
    • (1995) Protein Sci. , vol.4 , pp. 2032-2039
    • West, M.1    Hecht, M.2
  • 36
    • 0024279235 scopus 로고
    • Analysis and prediction of the differnt types of β-turn in proteins
    • Wilmot, C. M., and Thornton, J. M. (1988). Analysis and prediction of the differnt types of β-turn in proteins, J. Mol. Biol. 203, 221-232.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221-232
    • Wilmot, C.M.1    Thornton, J.M.2
  • 37
    • 0026565850 scopus 로고
    • A variable gap penalty function and feature weights for protein 3-D structure comparisons
    • Zhu, Z. Y., Sali, A., and Blundell, T. L. (1992). A variable gap penalty function and feature weights for protein 3-D structure comparisons, Protein Eng. 5, 43-51.
    • (1992) Protein Eng. , vol.5 , pp. 43-51
    • Zhu, Z.Y.1    Sali, A.2    Blundell, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.