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Volumn 2, Issue 2, 1996, Pages 75-90

The solution structure of the immunodominant and cell receptor binding regions of foot-and-mouth disease virus serotype A, variant A

Author keywords

FMDV; NMR spectroscopy; NOE constraints; RGD (Arg Gly Asp); Structure

Indexed keywords

FOOT-AND-MOUTH DISEASE VIRUS;

EID: 0030089428     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199603)2:2<75::AID-PSC49>3.0.CO;2-Z     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0019959784 scopus 로고
    • Protection against foot-and-mouth disease by immunisation with a chemically synthesised peptide predicted from the viral nucleotide sequence
    • J. L. Bittle, R. A. Houghten, H. Alexander, T. M. Shinnick J. G. Sutcliffe, R. A. Lerner, D. J. Rowlands and F. Brown (1982). Protection against foot-and-mouth disease by immunisation with a chemically synthesised peptide predicted from the viral nucleotide sequence. Nature, 298, 30-33.
    • (1982) Nature , vol.298 , pp. 30-33
    • Bittle, J.L.1    Houghten, R.A.2    Alexander, H.3    Shinnick, T.M.4    Sutcliffe, J.G.5    Lerner, R.A.6    Rowlands, D.J.7    Brown, F.8
  • 2
    • 0024639043 scopus 로고
    • The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid)
    • G. Fox, N. R. Parry, P. V. Barnett, B. McGinn, D. J. Rowlands and F. Brown (1989). The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J. Gen. Virol., 70, 625-637.
    • (1989) J. Gen. Virol. , vol.70 , pp. 625-637
    • Fox, G.1    Parry, N.R.2    Barnett, P.V.3    McGinn, B.4    Rowlands, D.J.5    Brown, F.6
  • 4
    • 0024578406 scopus 로고
    • The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
    • L. Acharya, E. Foy, D. Smart, G. Fox, D. Rowlands and F. Brown (1989). The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution. Nature, 337, 709-711.
    • (1989) Nature , vol.337 , pp. 709-711
    • Acharya, L.1    Foy, E.2    Smart, D.3    Fox, G.4    Rowlands, D.5    Brown, F.6
  • 8
    • 0026316368 scopus 로고
    • A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenic peptide
    • G. Siligardi, A. F. Drake, P. Mascagni, D. Rowlands, F. Brown and W. A. Gibbons (1991). A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenic peptide. Int. J Peptide Protein Res., 38, 519-527.
    • (1991) Int. J Peptide Protein Res. , vol.38 , pp. 519-527
    • Siligardi, G.1    Drake, A.F.2    Mascagni, P.3    Rowlands, D.4    Brown, F.5    Gibbons, W.A.6
  • 9
    • 0025737751 scopus 로고
    • Correlation between the conformations elucidated by CD spectroscopy and the antigenic properties of four peptides of the foot-and-mouth disease virus
    • G. Siligardi, A. F. Drake, P. Mascagni, D. Rowlands, F. Brown and W. A. Gibbons (1991b). Correlation between the conformations elucidated by CD spectroscopy and the antigenic properties of four peptides of the foot-and-mouth disease virus. Eur. J. Biochem., 199, 545-551.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 545-551
    • Siligardi, G.1    Drake, A.F.2    Mascagni, P.3    Rowlands, D.4    Brown, F.5    Gibbons, W.A.6
  • 10
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I Myohemerythrin
    • H. J. Dyson, G. Merutka, J. P. Waltho, R. A. Lerner and P. E. Wright (1992) Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I Myohemerythrin. J. Mol. Biol., 226, 795-817.
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 11
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I Plastocyanin
    • H. J. Dyson, J. R. Sayre, G. Merutka, H. C. Shin, R. A. Lerner and P. E. Wright (1992). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I Plastocyanin. J. Mol. Biol. 226, 819-835.
    • (1992) J. Mol. Biol. , vol.226 , pp. 819-835
    • Dyson, H.J.1    Sayre, J.R.2    Merutka, G.3    Shin, H.C.4    Lerner, R.A.5    Wright, P.E.6
  • 12
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • D. Sonnichsen, J. E. Van Eyk, R. S. Hodges and B. D. Sykes (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry, 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnichsen, D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 13
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensity from TFE titration curves
    • A. Jasonoff and A. R. Fersht (1994). Quantitative determination of helical propensity from TFE titration curves. Biochemistry, 33, 2129-2135.
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasonoff, A.1    Fersht, A.R.2
  • 14
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • D. K. Waterhouse and W. C. Johnson Jr (1994). Importance of environment in determining secondary structure in proteins. Biochemistry, 33, 2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhouse, D.K.1    Johnson Jr., W.C.2
  • 15
    • 0027981464 scopus 로고
    • Circular dichroism, molecular modeling and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is α-helix formation
    • L. L. France, P. G. Piatti, J. F. E. Newman, I. Toth, W. A. Gibbons and F. Brown (1994). Circular dichroism, molecular modeling and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is α-helix formation. Proc. Natl Acad. Sci. USA, 91, 8442-8446.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8442-8446
    • France, L.L.1    Piatti, P.G.2    Newman, J.F.E.3    Toth, I.4    Gibbons, W.A.5    Brown, F.6
  • 17
    • 49049123546 scopus 로고
    • The theory and practice of distance geometry
    • T. F. Havel, J. D. Kuntz and G. M. Crippen (1983). The theory and practice of distance geometry. Bull. Math. Biol 45, 655-720.
    • (1983) Bull. Math. Biol , vol.45 , pp. 655-720
    • Havel, T.F.1    Kuntz, J.D.2    Crippen, G.M.3
  • 19
    • 0000615669 scopus 로고
    • Function minimization by conjugate gradients
    • R. Fletcher and C. M. Reeves (1964). Function minimization by conjugate gradients. Comput. J., 7, 149-167.
    • (1964) Comput. J. , vol.7 , pp. 149-167
    • Fletcher, R.1    Reeves, C.M.2
  • 22
    • 0023762313 scopus 로고
    • Combined procedure of distance geometry and restrained molecular dynamics techniques for protein structure determination from nuclear magnetic resonance data: Application to the DNA binding domain of lac repressor from Escherichia coli
    • J. de Vlieg, R. M. Scheek, W. F. van Gunsteren, H. J. C. Berendsen, R. Kaptein and J. Thomason (1988). Combined procedure of distance geometry and restrained molecular dynamics techniques for protein structure determination from nuclear magnetic resonance data: application to the DNA binding domain of lac repressor from Escherichia coli. Proteins: Struct. Funct. Genet., 3, 209-218.
    • (1988) Proteins: Struct. Funct. Genet. , vol.3 , pp. 209-218
    • De Vlieg, J.1    Scheek, R.M.2    Van Gunsteren, W.F.3    Berendsen, H.J.C.4    Kaptein, R.5    Thomason, J.6
  • 24
    • 0003170076 scopus 로고
    • An alternative method for distance evaluation from NOESY spectra
    • G. Esposito and A. Pastore (1988). An alternative method for distance evaluation from NOESY spectra. J. Magn. Reson., 76, 331-336.
    • (1988) J. Magn. Reson. , vol.76 , pp. 331-336
    • Esposito, G.1    Pastore, A.2
  • 27
    • 0026909327 scopus 로고
    • Conformational study of a nine residue fragment of the antigenic loop of foot-and-mouth disease virus
    • M. C. Vega, C. Aleman, E. Giralt and J. J. Perez (1992). Conformational study of a nine residue fragment of the antigenic loop of foot-and-mouth disease virus. J. Biomol Struct. Dynamics, 10, 1-8.
    • (1992) J. Biomol Struct. Dynamics , vol.10 , pp. 1-8
    • Vega, M.C.1    Aleman, C.2    Giralt, E.3    Perez, J.J.4
  • 28
    • 0023339433 scopus 로고
    • Distance geometry and related methods for protein structure determination from NMR data
    • W. Braun (1987). Distance geometry and related methods for protein structure determination from NMR data. Q. Rev. Biophys., 19, 115-157.
    • (1987) Q. Rev. Biophys. , vol.19 , pp. 115-157
    • Braun, W.1
  • 29
    • 0017709445 scopus 로고
    • β-turn in proteins
    • P. Y. Chou and G. D. Fasman (1977). β-turn in proteins. J. Mol. Biol., 115, 135-175.
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-175
    • Chou, P.Y.1    Fasman, G.D.2
  • 32
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobia moment plot
    • D. Eisenberg, E. Schwartz, M. Komaramy and R. Wall (1984). Analysis of membrane and surface protein sequences with the hydrophobia moment plot. J. Mol. Biol., 179, 125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwartz, E.2    Komaramy, M.3    Wall, R.4
  • 33
    • 0024307675 scopus 로고
    • Neutralizing epitopes of type O foot-and-mouth disease virus. II. Mapping three conformational sites with synthetic peptide reagents
    • N. R. Parry, P. V. Barnett, E. J. Ouldridge, D. J. Rowlands and F. Brown (1989). Neutralizing epitopes of type O foot-and-mouth disease virus. II. Mapping three conformational sites with synthetic peptide reagents. J. Gen. Virol., 70, 1493-1503.
    • (1989) J. Gen. Virol. , vol.70 , pp. 1493-1503
    • Parry, N.R.1    Barnett, P.V.2    Ouldridge, E.J.3    Rowlands, D.J.4    Brown, F.5
  • 34
    • 0025094320 scopus 로고
    • Structural and serological evidence for a novel mechanism of antigenic variation in foot and mouth disease virus
    • N. P. Parry, G. Fox, D. Rowlands, F. Brown, E. Fry, R. Acharya, D. Logan and D. Stuart (1990). Structural and serological evidence for a novel mechanism of antigenic variation in foot and mouth disease virus. Nature, 347, 569-572.
    • (1990) Nature , vol.347 , pp. 569-572
    • Parry, N.P.1    Fox, G.2    Rowlands, D.3    Brown, F.4    Fry, E.5    Acharya, R.6    Logan, D.7    Stuart, D.8
  • 35
    • 0029019739 scopus 로고
    • Structure of the major antigenic loop of FMDV complexed with a neutralising antibody: Direct involvement of the RGD motif in the interaction
    • N. Verdaguer, M. G. Mateu, D. Andreu, E. Giralt, E. Domingo and I. Fita (1995) Structure of the major antigenic loop of FMDV complexed with a neutralising antibody: direct involvement of the RGD motif in the interaction. EMBO J:, 14, 1690-1696.
    • (1995) EMBO J , vol.14 , pp. 1690-1696
    • Verdaguer, N.1    Mateu, M.G.2    Andreu, D.3    Giralt, E.4    Domingo, E.5    Fita, I.6


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