메뉴 건너뛰기




Volumn 284, Issue 3, 1998, Pages 541-548

Protein similarities beyond disulphide bridge topology

Author keywords

Disulphide bonds; Disulphide rich proteins; Protein structure; Protein superimposition; Protein topology

Indexed keywords

CARBOXYPEPTIDASE; DEFENSIN; DISULFIDE; ENZYME INHIBITOR; EPIDERMAL GROWTH FACTOR; PHEROMONE; PLATELET DERIVED GROWTH FACTOR; SNAKE VENOM;

EID: 0032484157     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2194     Document Type: Article
Times cited : (35)

References (44)
  • 1
    • 0030707764 scopus 로고    scopus 로고
    • Bioinformatics: From genome data to biological knowledge
    • Andrade, M. A. & Sander, C. (1997). Bioinformatics: from genome data to biological knowledge. Curr. Opin. Biotechnol. 8, 675-683.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 675-683
    • Andrade, M.A.1    Sander, C.2
  • 2
    • 0027516469 scopus 로고
    • Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and the activation process
    • Avilés, F. X., Vendrell, J., Guash, A., Coll, M. & Huber, J. (1993). Advances in metallo-procarboxypeptidases. Emerging details on the inhibition mechanism and the activation process. Eur. J. Biochem. 211, 381-389.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 381-389
    • Avilés, F.X.1    Vendrell, J.2    Guash, A.3    Coll, M.4    Huber, J.5
  • 4
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • Betz, S. F. (1993). Disulfide bonds and the stability of globular proteins. Protein Sci. 2, 1551-1558.
    • (1993) Protein Sci. , vol.2 , pp. 1551-1558
    • Betz, S.F.1
  • 6
    • 0029348432 scopus 로고
    • BLAST, BLITZ, BLOCKS and BEAUTY: Sequence comparison on the net
    • Brenner, S. E. (1995). BLAST, BLITZ, BLOCKS and BEAUTY: sequence comparison on the net. Trends Genet. 11, 330-331.
    • (1995) Trends Genet. , vol.11 , pp. 330-331
    • Brenner, S.E.1
  • 7
    • 0026451624 scopus 로고
    • Nuclear magnetic resonance solution structure of the α-neurotoxin from Black Mamba
    • Brown, L. R. & Wüthrich, K. (1992). Nuclear magnetic resonance solution structure of the α-neurotoxin from Black Mamba. J. Mol. Biol. 227, 1118-1135.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1118-1135
    • Brown, L.R.1    Wüthrich, K.2
  • 8
    • 0024477288 scopus 로고
    • 1H assignment and secondary structure of human transforming growth factor α
    • 1H assignment and secondary structure of human transforming growth factor α. Biochemistry, 28, 593-599.
    • (1989) Biochemistry , vol.28 , pp. 593-599
    • Brown, S.C.1    Mueller, L.2    Jeffs, P.W.3
  • 9
    • 0028121986 scopus 로고
    • The disulfide folding pathway of potato carboxypeptidase inhibitor
    • Chang, J., Canals, F., Shindler, P., Querol, E. & Avilés, F. X. (1994). The disulfide folding pathway of potato carboxypeptidase inhibitor. J. Biol. Chem. 269, 33087-33094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33087-33094
    • Chang, J.1    Canals, F.2    Shindler, P.3    Querol, E.4    Avilés, F.X.5
  • 10
    • 0028911697 scopus 로고
    • The disulfide folding pathway of human epidermal growth factor
    • Chang, J., Shindler, P., Ramseier, U. & Lai, P. (1995). The disulfide folding pathway of human epidermal growth factor. J. Biol. Chem. 270, 9207-9216.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9207-9216
    • Chang, J.1    Shindler, P.2    Ramseier, U.3    Lai, P.4
  • 12
    • 0000552763 scopus 로고
    • Folding pathways determined using disulphide bonds
    • Creighton, T. E., ed., W. H. Freeman & Company, New York, USA
    • Creighton, T. E. (1992). Folding pathways determined using disulphide bonds. In Protein Folding (Creighton, T. E., ed.), pp. 301-351, W. H. Freeman & Company, New York, USA.
    • (1992) Protein Folding , pp. 301-351
    • Creighton, T.E.1
  • 13
    • 0032005344 scopus 로고    scopus 로고
    • Antimicrobial peptides of vertebrates
    • Ganzt, T. & Lehrer, R. I. (1998). Antimicrobial peptides of vertebrates. Curr. Opin. Immun. 10, 41-44.
    • (1998) Curr. Opin. Immun. , vol.10 , pp. 41-44
    • Ganzt, T.1    Lehrer, R.I.2
  • 14
    • 0028618937 scopus 로고
    • Structure-fuction relationships for the EGFT/TGF-α family of mitogens
    • Groenen, L. G., Nice, E. C. & Burgess, A. W. (1994). Structure-fuction relationships for the EGFT/TGF-α family of mitogens. Growth Factors, 11, 235-257.
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.G.1    Nice, E.C.2    Burgess, A.W.3
  • 15
    • 0030573025 scopus 로고    scopus 로고
    • The disulphide β-cross: From cysteine geometry and clustering to classification of small disulphide-rich protein folds
    • Harrison, P. & Sternberg, M. J. E. (1996). The disulphide β-cross: from cysteine geometry and clustering to classification of small disulphide-rich protein folds. J. Mol. Biol. 264, 603-623.
    • (1996) J. Mol. Biol. , vol.264 , pp. 603-623
    • Harrison, P.1    Sternberg, M.J.E.2
  • 16
    • 0025903814 scopus 로고
    • Crystal structure of Defensin HNP-3, an amphiphilic dimer: Mechanism of membrane permeabilization
    • Hill, C. P., Yee, J., Selsted, M. E. & Eisenberg, D. (1991). Crystal structure of Defensin HNP-3, an amphiphilic dimer: mechanism of membrane permeabilization. Science, 251, 1481-1485.
    • (1991) Science , vol.251 , pp. 1481-1485
    • Hill, C.P.1    Yee, J.2    Selsted, M.E.3    Eisenberg, D.4
  • 17
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm, U. & Sander, C. (1994). Enlarged representative set of protein structures. Protein Sci. 3, 522-524.
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 18
    • 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. 223, 123-138.
    • (1993) J. Mol. Biol. , vol.223 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 22
    • 0029392391 scopus 로고
    • A disulphide-reinforced structural scaffold shared by small proteins with diverse functions
    • Lin, S. L. & Nussinov, R. (1995). A disulphide-reinforced structural scaffold shared by small proteins with diverse functions. Nature Struct. Biol. 2, 835-837.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 835-837
    • Lin, S.L.1    Nussinov, R.2
  • 23
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon, R., Cohen, S. T., Kuo, A., Lee, A. & Chait, B. T. (1998). Structural conservation in prokaryotic and eukaryotic potassium channels. Science, 280, 106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.T.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 24
    • 0032553333 scopus 로고    scopus 로고
    • Refolding of potato carboxypeptidase inhibitor by molecular dynamics simulations with disulphide bond constraints
    • Martí-Renom, M. A., Stote, R. H., Querol, E., Avilés, F. X. & Karplus, M. (1998). Refolding of potato carboxypeptidase inhibitor by molecular dynamics simulations with disulphide bond constraints. J. Mol. Biol. 284, 145-172.
    • (1998) J. Mol. Biol. , vol.284 , pp. 145-172
    • Martí-Renom, M.A.1    Stote, R.H.2    Querol, E.3    Avilés, F.X.4    Karplus, M.5
  • 25
    • 0022272122 scopus 로고
    • Comparison of protein structures
    • Matthews, B. W. & Rossmann, M. G. (1985). Comparison of protein structures. Methods Enzymol. 115, 397-420.
    • (1985) Methods Enzymol. , vol.115 , pp. 397-420
    • Matthews, B.W.1    Rossmann, M.G.2
  • 26
    • 0027932407 scopus 로고
    • The C-tail valine is a key residue for the stabilization of the complex between potato inhibitor and carboxypeptidase A
    • Molina, M. A., Marino, C., Oliva, B., Avilés, F. X. & Querol, E. (1994). The C-tail valine is a key residue for the stabilization of the complex between potato inhibitor and carboxypeptidase A. J. Biol. Chem. 269, 21467-21472.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21467-21472
    • Molina, M.A.1    Marino, C.2    Oliva, B.3    Avilés, F.X.4    Querol, E.5
  • 27
    • 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. (1995). SCOP a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 28
    • 0025728989 scopus 로고
    • On the stability and fluctuations of the potato carboxypeptidase inhibitor fold: A molecular dynamics study
    • Oliva, B., Wastlund, M., Cardenas, R., Querol, E., Avilés, F. X. & Tapia, O. (1991a). On the stability and fluctuations of the potato carboxypeptidase inhibitor fold: a molecular dynamics study. Biochem. Biophys. Res. Commun. 176, 616-621.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 616-621
    • Oliva, B.1    Wastlund, M.2    Cardenas, R.3    Querol, E.4    Avilés, F.X.5    Tapia, O.6
  • 29
    • 0025755629 scopus 로고
    • Aspects of model building applied to carboxypeptidase inhibitor protein: A molecular dynamics study of a putative Pro36/Gly mutant
    • Oliva, B., Wastlund, M. ,Nilssonn O., Cardenas, R., Avilés, F. X., Querol, E. & Tapia, O. (1991b). Aspects of model building applied to carboxypeptidase inhibitor protein: a molecular dynamics study of a putative Pro36/Gly mutant. Biochem. Biophys. Res. Commun. 176, 627-637.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 627-637
    • Oliva, B.1    Wastlund, M.2    Nilssonn, O.3    Cardenas, R.4    Avilés, F.X.5    Querol, E.6    Tapia, O.7
  • 30
    • 0029077590 scopus 로고
    • Structure and fluctuation patterns of potato carboxypeptidase A inhibitor protein in aqueous solution. A molecular dynamics study
    • Oliva, B., Daura, X., Nilsson, O., Querol, E., Avilés, F. X. & Tapia, O. (1995). Structure and fluctuation patterns of potato carboxypeptidase A inhibitor protein in aqueous solution. A molecular dynamics study. Eur. Biophys. J. 24, 1-12.
    • (1995) Eur. Biophys. J. , vol.24 , pp. 1-12
    • Oliva, B.1    Daura, X.2    Nilsson, O.3    Querol, E.4    Avilés, F.X.5    Tapia, O.6
  • 31
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostanglandin H2 synthase-1
    • Picot, D., Loll, P. J. & Garavito, R. M. (1994). The X-ray crystal structure of the membrane protein prostanglandin H2 synthase-1. Nature, 367, 243-249.
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 32
    • 0020491126 scopus 로고
    • Refined crystal structure of the potato carboxypeptidase inhibitor complex of carboxypeptidase A at 2.5 Å resolution
    • Rees, D. C. & Lipscomb, W. N. (1982). Refined crystal structure of the potato carboxypeptidase inhibitor complex of carboxypeptidase A at 2.5 Å resolution. J. Mol. Biol. 160, 475-498.
    • (1982) J. Mol. Biol. , vol.160 , pp. 475-498
    • Rees, D.C.1    Lipscomb, W.N.2
  • 33
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981). The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34, 167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 34
    • 0017187837 scopus 로고
    • Exploring structural homology of proteins
    • Rossmann, M. G. & Argos, P. (1976). Exploring structural homology of proteins. J. Mol. Biol. 105, 75-95.
    • (1976) J. Mol. Biol. , vol.105 , pp. 75-95
    • Rossmann, M.G.1    Argos, P.2
  • 35
    • 0030627901 scopus 로고    scopus 로고
    • Protein structures sustain evolutionary drift
    • Rost, B. (1997). Protein structures sustain evolutionary drift. Folding Design, 2, S19-20.
    • (1997) Folding Design , vol.2
    • Rost, B.1
  • 37
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation
    • Russell, R. B., Saqi, M. A. S., Sayle, R. A., Bates, P. A. & Sternberg, M. J. E. (1997). Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation. J. Mol. Biol. 269, 423-439.
    • (1997) J. Mol. Biol. , vol.269 , pp. 423-439
    • Russell, R.B.1    Saqi, M.A.S.2    Sayle, R.A.3    Bates, P.A.4    Sternberg, M.J.E.5
  • 38
    • 0029969880 scopus 로고    scopus 로고
    • Structural aspect of the functional modules in C-alpha deduced from comparative analysis
    • Srinivasan, N., Bax, B., Blundell, T. L. & Parker, P. J. (1996). Structural aspect of the functional modules in C-alpha deduced from comparative analysis. Proteins: Struct. Funct. Genet. 26, 217-235.
    • (1996) Proteins: Struct. Funct. Genet. , vol.26 , pp. 217-235
    • Srinivasan, N.1    Bax, B.2    Blundell, T.L.3    Parker, P.J.4
  • 39
    • 0024349252 scopus 로고
    • Protein structure alignment
    • Taylor, W. R. & Orengo, C. (1989). Protein structure alignment. J. Mol. Biol. 208, 1-22.
    • (1989) J. Mol. Biol. , vol.208 , pp. 1-22
    • Taylor, W.R.1    Orengo, C.2
  • 40
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton, J. M. (1981). Disulphide bridges in globular proteins. J. Mol. Biol. 151, 261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 41
    • 0026630971 scopus 로고
    • Three-dimensional structure of the apo form of the N-terminal EGF-Like module of blood coagulation factor X as determined by NMR spectrocopy an simulated folding
    • Ullner, M., Selander, M., Persson, E., Stenflo, J., Drakenberg, T. & Teleman, O. (1992). Three-dimensional structure of the apo form of the N-terminal EGF-Like module of blood coagulation factor X as determined by NMR spectrocopy an simulated folding. Biochemistry, 31, 5974-5983.
    • (1992) Biochemistry , vol.31 , pp. 5974-5983
    • Ullner, M.1    Selander, M.2    Persson, E.3    Stenflo, J.4    Drakenberg, T.5    Teleman, O.6
  • 42
    • 0028049805 scopus 로고
    • A peptide that stimulates phosphorylation of the plant insulin-binding protein. Isolation, primary structure and cDNA cloning
    • Watanabe, Y., Barbashov, S. F., Komatsu, S., Hemmings, A. M., Miyagi, M., Tsunasawa, S. & Hirano, H. (1994). A peptide that stimulates phosphorylation of the plant insulin-binding protein. Isolation, primary structure and cDNA cloning. Eur. J. Biochem. 224, 167-172.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 167-172
    • Watanabe, Y.1    Barbashov, S.F.2    Komatsu, S.3    Hemmings, A.M.4    Miyagi, M.5    Tsunasawa, S.6    Hirano, H.7
  • 43
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White, S. H., Wimley, W. C. & Selsted, M. H. (1995). Structure, function, and membrane integration of defensins. Curr. Opin. Struct. Biol. 5, 521-527.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.H.3
  • 44
    • 0031954924 scopus 로고    scopus 로고
    • Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry
    • Wu, J., Yang, Y. & Watson, J. T. (1998). Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry. Protein Sci. 7, 1017-1028.
    • (1998) Protein Sci. , vol.7 , pp. 1017-1028
    • Wu, J.1    Yang, Y.2    Watson, J.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.