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Volumn 162, Issue 1, 1999, Pages 331-337

Extensive alanine substitutions increase binding affinity of an influenza nucleoprotein peptide to HLA-Aw68 and do not abrogate peptide- specific CTL recognition

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; HLA A ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; SYNTHETIC PEPTIDE; VIRUS NUCLEOPROTEIN;

EID: 0032961106     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (22)
  • 1
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden, D. R., J. C. Gorga, J. L. Strominger, and D. C. Wiley. 1992. The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC. Cell 70:1035.
    • (1992) Cell , vol.70 , pp. 1035
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 2
    • 0024345149 scopus 로고
    • Specificity pockets for the side chains of peptide antigens in HLA-Aw68
    • Garrett, T P., M. A. Saper, P. J. Bjorkman, J. L. Strominger, and D. C. Wiley. 1989. Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature 342:692.
    • (1989) Nature , vol.342 , pp. 692
    • Garrett, T.P.1    Saper, M.A.2    Bjorkman, P.J.3    Strominger, J.L.4    Wiley, D.C.5
  • 3
    • 0026618817 scopus 로고
    • Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle
    • Guo, H. C., T. S. Jardetzky, T. P. Garrett, W. S. Lane, J. L. Strominger, and D. C. Wiley. 1992. Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360:364.
    • (1992) Nature , vol.360 , pp. 364
    • Guo, H.C.1    Jardetzky, T.S.2    Garrett, T.P.3    Lane, W.S.4    Strominger, J.L.5    Wiley, D.C.6
  • 4
    • 0028131363 scopus 로고
    • Importance of antigenic peptide N- and C-termini to the stability of class I MHC molecules
    • Bouvier, M., and D. C. Wiley. 1994. Importance of antigenic peptide N- and C-termini to the stability of class I MHC molecules. Science 265:398.
    • (1994) Science , vol.265 , pp. 398
    • Bouvier, M.1    Wiley, A.D.C.2
  • 6
    • 0026709414 scopus 로고
    • 2-microglobulin dissociation rate is an accurate measure of the stability of MHC class I heterotrimers and depends on which peptide is bound
    • 2-microglobulin dissociation rate is an accurate measure of the stability of MHC class I heterotrimers and depends on which peptide is bound. J. Immunol. 149:1896.
    • (1992) J. Immunol. , vol.149 , pp. 1896
    • Parker, K.C.1    DiBrino, M.2    Hull, L.3    Coligan, J.E.4
  • 7
    • 0027304399 scopus 로고
    • Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
    • Ruppert, J., J. Sidney, E. Celis, R. T. Kubo, H. M. Grey, and A. Sette. 1993. Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules. Cell 74:929.
    • (1993) Cell , vol.74 , pp. 929
    • Ruppert, J.1    Sidney, J.2    Celis, E.3    Kubo, R.T.4    Grey, H.M.5    Sette, A.6
  • 9
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the α 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith, K. J., S. W. Reid, D. I. Stuart, A. J. McMichael, E. Y. Jones, and J. I. Bell. 1996. An altered position of the α 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4:203.
    • (1996) Immunity , vol.4 , pp. 203
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 10
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • published erratum appears in 1994, Cell 76:410
    • Madden, D. R., D. N. Garboczi, and D. C. Wiley. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2 [published erratum appears in 1994, Cell 76:410]. Cell 75:693.
    • (1993) Cell , vol.75 , pp. 693
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 11
    • 0028871148 scopus 로고
    • The three-dimensional structure of a class I major histocompatibility complex molecule missing the α 3 domain of the heavy chain
    • Collins, E. J., D. N. Garboczi, M. N. Karpusas, and D. C. Wiley. 1995. The three-dimensional structure of a class I major histocompatibility complex molecule missing the α 3 domain of the heavy chain. Proc. Natl. Acad. Sci. USA 92:1218.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1218
    • Collins, E.J.1    Garboczi, D.N.2    Karpusas, M.N.3    Wiley, D.C.4
  • 12
    • 0028267613 scopus 로고
    • Naturally processed peptides longer than nine amino acid residues bind to the class I MHC molecule HLA-A2.1 with high affinity and in different conformations
    • Chen, Y., J. Sidney, S. Southwood, A. L. Cox, K. Sakaguchi, R. A. Henderson, E. Appella, D. F. Hunt, A. Sette, and V. H. Engelhard. 1994. Naturally processed peptides longer than nine amino acid residues bind to the class I MHC molecule HLA-A2.1 with high affinity and in different conformations. J. Immunol. 152:2874.
    • (1994) J. Immunol. , vol.152 , pp. 2874
    • Chen, Y.1    Sidney, J.2    Southwood, S.3    Cox, A.L.4    Sakaguchi, K.5    Henderson, R.A.6    Appella, E.7    Hunt, D.F.8    Sette, A.9    Engelhard, V.H.10
  • 13
    • 0028150789 scopus 로고
    • Three-dimensional structure of a peptide extending from one end of a class I MHC binding site
    • Collins, E. J., D. N. Garboczi, and D. C. Wiley. 1994. Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature 371:626.
    • (1994) Nature , vol.371 , pp. 626
    • Collins, E.J.1    Garboczi, D.N.2    Wiley, D.C.3
  • 15
    • 0029969665 scopus 로고    scopus 로고
    • Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53
    • Smith, K. J., S. W. Reid, K. Harlos, A. J. McMichael, D. I. Stuart, J. I. Bell, and E. Y. Jones. 1996. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity 4:215.
    • (1996) Immunity , vol.4 , pp. 215
    • Smith, K.J.1    Reid, S.W.2    Harlos, K.3    McMichael, A.J.4    Stuart, D.I.5    Bell, J.I.6    Jones, E.Y.7
  • 17
    • 0022483534 scopus 로고
    • The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides
    • Townsend, A. R., J. Rothbard, F. M. Gotch, G. Bahadur, D. Wraith, and A. J. McMichael. 1986. The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides. Cell 44:959.
    • (1986) Cell , vol.44 , pp. 959
    • Townsend, A.R.1    Rothbard, J.2    Gotch, F.M.3    Bahadur, G.4    Wraith, D.5    McMichael, A.J.6
  • 18
    • 0023256436 scopus 로고
    • Cytotoxic T lymphocytes recognize a fragment of influenza virus matrix protein in association with HLA-A2
    • Gotch, F., J. Rothbard, K. Howland, A. Townsend, and A. McMichael. 1987. Cytotoxic T lymphocytes recognize a fragment of influenza virus matrix protein in association with HLA-A2. Nature 326:881.
    • (1987) Nature , vol.326 , pp. 881
    • Gotch, F.1    Rothbard, J.2    Howland, K.3    Townsend, A.4    McMichael, A.5
  • 21
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • Saper, M. A., P. J. Bjorkman, and D. C. Wiley. 1991. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J. Mol. Biol. 219:277.
    • (1991) J. Mol. Biol. , vol.219 , pp. 277
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.