메뉴 건너뛰기




Volumn 27, Issue 2, 1997, Pages 279-289

A predicted consensus structure for the C terminus of the beta and gamma chains of fibrinogen

Author keywords

CASP2; compensatory covariation; prediction contest; protein sequence alignment; protein structure prediction

Indexed keywords

FIBRINOGEN;

EID: 0031042554     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199702)27:2<279::AID-PROT13>3.0.CO;2-J     Document Type: Article
Times cited : (4)

References (35)
  • 1
    • 0024839793 scopus 로고
    • Patterns of divergence in homologous proteins as indicators of tertiary and quaternary structure
    • Benner, S.A. Patterns of divergence in homologous proteins as indicators of tertiary and quaternary structure. Adv. Enzymol. Reg. 28:219-236, 1989.
    • (1989) Adv. Enzymol. Reg. , vol.28 , pp. 219-236
    • Benner, S.A.1
  • 3
    • 0026772714 scopus 로고
    • Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains
    • Russell, R.B., Breed, J., Barton, G.J. Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains. FEBS Lett. 304;1520, 1992.
    • (1992) FEBS Lett. , vol.304 , pp. 1520
    • Russell, R.B.1    Breed, J.2    Barton, G.J.3
  • 4
    • 0026749753 scopus 로고
    • SH3: An abundant protein domain in search of a function
    • Musacchio, A., Gibson, T., Lehto, V.-P., Saraste, M. SH3: An abundant protein domain in search of a function. FEBS Lett. 307:55-61, 1992.
    • (1992) FEBS Lett. , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.-P.3    Saraste, M.4
  • 5
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J.F. Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl. Acad. Sci. USA 87:6934-6937, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6934-6937
    • Bazan, J.F.1
  • 7
    • 0027943361 scopus 로고
    • Predicting protein crystal structures
    • Benner, S.A., Gerloff, D.L., Jenny, T.F. Predicting protein crystal structures. Science 265:1642-1644, 1994.
    • (1994) Science , vol.265 , pp. 1642-1644
    • Benner, S.A.1    Gerloff, D.L.2    Jenny, T.F.3
  • 8
    • 0002043872 scopus 로고
    • Evolution and structural theory: The frontier between chemistry and biochemistry
    • Benner, S.A., Ellington, A.D. Evolution and structural theory: The frontier between chemistry and biochemistry. Bioorg. Chem. Front. 1:1-70, 1990.
    • (1990) Bioorg. Chem. Front. , vol.1 , pp. 1-70
    • Benner, S.A.1    Ellington, A.D.2
  • 9
    • 0343810443 scopus 로고    scopus 로고
    • Predicting the conformation of proteins from sequence data
    • Craik, C.S., Cleland, J. (eds.)
    • Benner, S.A. Predicting the conformation of proteins from sequence data. In "Protein Engineering: A Guide to Design and Production." Craik, C.S., Cleland, J. (eds.). 1996:71-99.
    • (1996) Protein Engineering: A Guide to Design and Production , pp. 71-99
    • Benner, S.A.1
  • 10
    • 0022706389 scopus 로고    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.
    • EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 11
    • 0343810442 scopus 로고    scopus 로고
    • Bona fide predictions of protein secondary structure using transparent analyses of multiple sequence alignments
    • submitted
    • Benner, S.A., Chelvanayagam, G., Turcotte, M. Bona fide predictions of protein secondary structure using transparent analyses of multiple sequence alignments. Chem. Rev., submitted, 1996.
    • (1996) Chem. Rev.
    • Benner, S.A.1    Chelvanayagam, G.2    Turcotte, M.3
  • 12
    • 0028359958 scopus 로고
    • Evaluating predictions of secondary structure in proteins
    • Jenny, T.F., Benner, S.A. Evaluating predictions of secondary structure in proteins. Biochem. Biophys. Res. Commun. 200:149-155, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 149-155
    • Jenny, T.F.1    Benner, S.A.2
  • 13
    • 0027933115 scopus 로고
    • A prediction of the secondary structure of the pleckstrin homology domain
    • Jenny, T.F., Benner, S.A. A prediction of the secondary structure of the pleckstrin homology domain. Proteins 20: 1-4, 1994.
    • (1994) Proteins , vol.20 , pp. 1-4
    • Jenny, T.F.1    Benner, S.A.2
  • 14
    • 0027183541 scopus 로고
    • The PH domain: A common piece in the structural patchwork of signaling proteins
    • Musacchio, A., Gibson, T., Rice, P., Thompson, J., Sarasate M. The PH domain: A common piece in the structural patchwork of signaling proteins. Trends Biochem. Sci. 18: 343-348, 1993.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Rice, P.3    Thompson, J.4    Sarasate, M.5
  • 16
    • 0028801403 scopus 로고
    • The phospho-beta-galactosidase and synaptotagmin predictions
    • Benner, S.A., Gerloff, D.L., Chelvanayagam, G. The phospho-beta-galactosidase and synaptotagmin predictions. Proteins 23:446-453, 1995.
    • (1995) Proteins , vol.23 , pp. 446-453
    • Benner, S.A.1    Gerloff, D.L.2    Chelvanayagam, G.3
  • 17
    • 0342505241 scopus 로고    scopus 로고
    • Helix fold prediction for the cyclin box
    • Bazan, J.F. Helix fold prediction for the cyclin box. Proteins 24:18-34, 1996.
    • (1996) Proteins , vol.24 , pp. 18-34
    • Bazan, J.F.1
  • 18
    • 0028959231 scopus 로고
    • The protein fold of the von Willebrand factor type a domain is predicted to be similar to the open twisted beta-sheet flanked by alpha helices found in human Ras-p21
    • Edwards, Y.J.K., Perkins, S.J. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted beta-sheet flanked by alpha helices found in human Ras-p21. FEBS Lett. 358:283-286, 1995.
    • (1995) FEBS Lett. , vol.358 , pp. 283-286
    • Edwards, Y.J.K.1    Perkins, S.J.2
  • 19
    • 0028872390 scopus 로고
    • Predicted secondary and supersecondary structure for the serine/threonine specific protein phosphatase family
    • Jenny, T.F., Gerloff, D.L., Cohen, M.A., Benner, S.A. Predicted secondary and supersecondary structure for the serine/threonine specific protein phosphatase family. Proteins 21:1-10, 1995.
    • (1995) Proteins , vol.21 , pp. 1-10
    • Jenny, T.F.1    Gerloff, D.L.2    Cohen, M.A.3    Benner, S.A.4
  • 20
    • 0028059023 scopus 로고
    • Secondary structure prediction from multiple sequence data: Blood clotting factor XIII and Yersinia protein-tyrosine phosphatase
    • Livinston, C.D., Barton, G.J. Secondary structure prediction from multiple sequence data: Blood clotting factor XIII and Yersinia protein-tyrosine phosphatase. Int. J. Peptide Protein Res. 44:239-244, 1994.
    • (1994) Int. J. Peptide Protein Res. , vol.44 , pp. 239-244
    • Livinston, C.D.1    Barton, G.J.2
  • 21
    • 0028109452 scopus 로고
    • Predicted seconday structure of the 20 S proteasome and model structure of the putative peptide channel
    • Lupas, A., Koster, A.J., Walz, J., Baumeister, W. Predicted seconday structure of the 20 S proteasome and model structure of the putative peptide channel. FEBS Lett. 354: 45-49, 1994.
    • (1994) FEBS Lett. , vol.354 , pp. 45-49
    • Lupas, A.1    Koster, A.J.2    Walz, J.3    Baumeister, W.4
  • 22
  • 23
  • 24
    • 0026562263 scopus 로고
    • The SWISS-PROT protein sequence data bank
    • Bairoch, A., Boeckmann, B. The SWISS-PROT protein sequence data bank. Nucleic Acids Res. 20:2019-2022, 1992.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2019-2022
    • Bairoch, A.1    Boeckmann, B.2
  • 26
    • 0026656815 scopus 로고
    • Exhaustive matching of the entire protein sequence dtabase
    • Gonnet, G.H., Cohen, M.A., Benner, S.A. Exhaustive matching of the entire protein sequence dtabase. Science 256:1443-1445, 1992.
    • (1992) Science , vol.256 , pp. 1443-1445
    • Gonnet, G.H.1    Cohen, M.A.2    Benner, S.A.3
  • 27
    • 0028180367 scopus 로고
    • Bona fide prediction of aspects of protein conformation: Assigning interior and surface residues from patterns of variation and conservation in homologous protein sequences
    • Benner, S.A., Badcoe, I., Cohen, M.A., Gerloff, D.L. Bona fide prediction of aspects of protein conformation: Assigning interior and surface residues from patterns of variation and conservation in homologous protein sequences. J. Mol. Biol. 235:926-958, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 926-958
    • Benner, S.A.1    Badcoe, I.2    Cohen, M.A.3    Gerloff, D.L.4
  • 28
    • 0025935158 scopus 로고    scopus 로고
    • Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: The catalytic domain of protein kinases
    • 191
    • Benner, S.A., Gerloff, D. Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: The catalytic domain of protein kinases. Adv. Enzymol. Reg. 31:121-181, 191.
    • Adv. Enzymol. Reg. , vol.31 , pp. 121-181
    • Benner, S.A.1    Gerloff, D.2
  • 29
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Göbel, U., Sander, C., Schneider, R., Valencia, A. Correlated mutations and residue contacts in proteins. Proteins 18:309-317, 1994.
    • (1994) Proteins , vol.18 , pp. 309-317
    • Göbel, U.1    Sander, C.2    Schneider, R.3    Valencia, A.4
  • 30
    • 0028125904 scopus 로고
    • How frequent are correlated changes in families of protein sequences?
    • Neher, E. How frequent are correlated changes in families of protein sequences? Proc. Natl. Acad. Sci. USA 91:98-102, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 98-102
    • Neher, E.1
  • 31
    • 0028084754 scopus 로고
    • Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations?
    • Shindyalov, I.N., Kolchanov, N.A., Sander, C. Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations? Protein Eng. 7:349-358, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 349-358
    • Shindyalov, I.N.1    Kolchanov, N.A.2    Sander, C.3
  • 32
    • 0027952860 scopus 로고
    • Compensating changes in protein multiple sequence alignments
    • Taylor, W.R., Hatrick, K.L. Compensating changes in protein multiple sequence alignments. Protein Eng. 7:341-348, 1994.
    • (1994) Protein Eng. , vol.7 , pp. 341-348
    • Taylor, W.R.1    Hatrick, K.L.2
  • 34
    • 0030054216 scopus 로고    scopus 로고
    • Improving protein secondary structure prediction with aligned homologous sequences
    • di Francesco, V., Gamier, J., Munson, P.J. Improving protein secondary structure prediction with aligned homologous sequences. Protein Sci. 5:106-113, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 106-113
    • Di Francesco, V.1    Gamier, J.2    Munson, P.J.3
  • 35
    • 0027055525 scopus 로고
    • A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives
    • Doolittle, R.F. A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Sci. 1:1563-1577, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 1563-1577
    • Doolittle, R.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.