메뉴 건너뛰기




Volumn 260, Issue 4, 1996, Pages 604-620

A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique

Author keywords

Dataset of subunit interfaces; Hydrophobic interactions; Protein cores; Protein folding; Protein protein recognition

Indexed keywords

INTERLEUKIN 8; LACTATE DEHYDROGENASE; MACROPHAGE INFLAMMATORY PROTEIN 1; MONOCLONAL ANTIBODY; MUTANT PROTEIN;

EID: 0030602896     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0424     Document Type: Article
Times cited : (151)

References (26)
  • 1
    • 0026587854 scopus 로고
    • Common spatial arrangements of back-bone fragments in homologous and non-homologous proteins
    • Alexandrov, N. N., Takahashi, K. & Go, N. (1992). Common spatial arrangements of back-bone fragments in homologous and non-homologous proteins. J. Mol. Biol. 225, 5-9.
    • (1992) J. Mol. Biol. , vol.225 , pp. 5-9
    • Alexandrov, N.N.1    Takahashi, K.2    Go, N.3
  • 2
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos, P. (1988). An investigation of protein subunit and domain interfaces. Protein Eng. 2, 101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 3
    • 0027238108 scopus 로고
    • A computer vision based technique for 3-D sequence independent structural comparison of proteins
    • Bachar, O., Fischer, D., Nussinov, R. & Wolfson. H. (1993). A computer vision based technique for 3-D sequence independent structural comparison of proteins. Protein Eng. 6, 279-288.
    • (1993) Protein Eng. , vol.6 , pp. 279-288
    • Bachar, O.1    Fischer, D.2    Nussinov, R.3    Wolfson, H.4
  • 7
    • 0028582135 scopus 로고
    • Analysis of hydrophobicity in the α and β chemokine families and its relevance to dimerization
    • Covell, D. G., Smythers, G. W., Gronenborn, A. M. & Clore, G. M. (1995). Analysis of hydrophobicity in the α and β chemokine families and its relevance to dimerization. Protein Sci. 3, 2064-2072.
    • (1995) Protein Sci. , vol.3 , pp. 2064-2072
    • Covell, D.G.1    Smythers, G.W.2    Gronenborn, A.M.3    Clore, G.M.4
  • 8
    • 0026802451 scopus 로고
    • Crystal structure of a streptococcal protein G domain bound to a Fab fragment
    • Derrick, J. P. & Wigley, D. B. (1992). Crystal structure of a streptococcal protein G domain bound to a Fab fragment. Nature, 359, 752-754.
    • (1992) Nature , vol.359 , pp. 752-754
    • Derrick, J.P.1    Wigley, D.B.2
  • 9
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle, R. F. (1994). Convergent evolution: the need to be explicit. Trends Biochem. Sci. 19, 15-18.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 10
    • 0028230909 scopus 로고
    • 3-D, sequence-order independent structural comparison of trypsin against the crystallographic database reveals active site similarities to subtilisin-like and sulfhydryl proteases: Potential implications
    • Fischer, D., Wolfson, H., Lin, S. L. & Nussinov, R. (1994). 3-D, sequence-order independent structural comparison of trypsin against the crystallographic database reveals active site similarities to subtilisin-like and sulfhydryl proteases: potential implications. Protein Sci. 3, 769-778.
    • (1994) Protein Sci. , vol.3 , pp. 769-778
    • Fischer, D.1    Wolfson, H.2    Lin, S.L.3    Nussinov, R.4
  • 11
    • 0029564871 scopus 로고
    • A 3-D sequence-independent representation of the protein data bank
    • Fischer, D., Tsai, C. J., Nussinov, R. & Wolfson, H. (1995). A 3-D sequence-independent representation of the protein data bank. Protein Eng. 8, 981-997.
    • (1995) Protein Eng. , vol.8 , pp. 981-997
    • Fischer, D.1    Tsai, C.J.2    Nussinov, R.3    Wolfson, H.4
  • 12
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 14
    • 0028773905 scopus 로고
    • The molecular structure of the complex of Ascaris chymotrypsin/ elastase inhibitor with porcine elastase
    • Huang, K., Strynadka, N. C. J., Bernard, V. D., Peanasky, R. J. & James, M. N. G. (1994). The molecular structure of the complex of Ascaris chymotrypsin/ elastase inhibitor with porcine elastase. Structure, 2, 679-689.
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Strynadka, N.C.J.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.G.5
  • 15
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J. & Chothia, C. (1990). The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 16
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S. & Chothia, C. (1988). Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204, 155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 17
    • 0028318094 scopus 로고
    • Factors influencing the ability of knowledge-based potentials to identify native sequence-structure motifs
    • Kocher, J.-P. A., Rooman, M. J. & Wodak, S. J. (1994). Factors influencing the ability of knowledge-based potentials to identify native sequence-structure motifs. J. Mol. Biol. 235, 1598-1613.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1598-1613
    • Kocher, J.-P.A.1    Rooman, M.J.2    Wodak, S.J.3
  • 18
    • 0012083240 scopus 로고
    • A study of four-helix bundles: Investigating protein folding via similar architechtural motifs in protein cores and in subunit interfaces
    • Lin, S. L., Tsai, C.-J. & Nussinov, R. (1995). A study of four-helix bundles: Investigating protein folding via similar architechtural motifs in protein cores and in subunit interfaces. J. Mol. Biol. 112, 535-542.
    • (1995) J. Mol. Biol. , vol.112 , pp. 535-542
    • Lin, S.L.1    Tsai, C.-J.2    Nussinov, R.3
  • 20
    • 0027155448 scopus 로고
    • A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5
    • Milburn, M. V., Hassell, A. M., Lambert, M. H., Jordan, S. R., Proudfoot, A. E. I., Graber, P. & Wells, T. N. C. (1993). A novel dimer configuration revealed by the crystal structure at 2.4 Å resolution of human interleukin-5. Nature, 363, 172-176.
    • (1993) Nature , vol.363 , pp. 172-176
    • Milburn, M.V.1    Hassell, A.M.2    Lambert, M.H.3    Jordan, S.R.4    Proudfoot, A.E.I.5    Graber, P.6    Wells, T.N.C.7
  • 21
    • 0025719208 scopus 로고
    • Efficient detection of three-dimensional structural motifs in biological macromolecules by computer vision techniques
    • Nussinov, R. & Wolfson, H. J. (1991). Efficient detection of three-dimensional structural motifs in biological macromolecules by computer vision techniques. Proc. Natl Acad. Sci. USA, 88, 10495-10499.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10495-10499
    • Nussinov, R.1    Wolfson, H.J.2
  • 23
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J. J. & Craik, C. S. (1995). Structural basis of substrate specificity in the serine proteases. Protein Sci. 4, 337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 24
    • 0029119320 scopus 로고
    • A preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor design
    • Wallqvist, A., Jernigan, R. L. & Covell, D. G. (1995). A preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor design. Protein Sci. 9, 1881-1903.
    • (1995) Protein Sci. , vol.9 , pp. 1881-1903
    • Wallqvist, A.1    Jernigan, R.L.2    Covell, D.G.3
  • 25
    • 0026464639 scopus 로고
    • New algorithm to model protein-protein recognition based on surface complementarity; Application to antibody-antigen docking
    • Walls, P. H. & Sternberg, M. J. E. (1992). New algorithm to model protein-protein recognition based on surface complementarity; Application to antibody-antigen docking. J. Mol. Biol. 228, 277-297.
    • (1992) J. Mol. Biol. , vol.228 , pp. 277-297
    • Walls, P.H.1    Sternberg, M.J.E.2
  • 26
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L., Jernigan, R. L. & Covell, D. G. (1994). A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 3, 717-729.
    • (1994) Protein Sci. , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.