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Volumn 45, Issue 2, 1996, Pages 121-129

Refined peptide HLA-B(*)3501 binding motif reveals differences in 9-mer to 11-mer peptide binding

Author keywords

[No Author keywords available]

Indexed keywords

HLA B ANTIGEN; T LYMPHOCYTE ANTIGEN; VIRUS PROTEIN;

EID: 0029841747     PISSN: 00937711     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002510050179     Document Type: Article
Times cited : (19)

References (37)
  • 1
    • 0028131363 scopus 로고
    • Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules
    • Bouvier, M. and Wiley, D. C. Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules. Science 265: 398-402, 1994
    • (1994) Science , vol.265 , pp. 398-402
    • Bouvier, M.1    Wiley, D.C.2
  • 2
    • 0028267613 scopus 로고
    • Naturally processed peptides longer than nine amino acid residues bind to class I MHC molecule HLA-A2.1 with high affinity and in different conformations
    • Chen, Y., Sidney, J., Southwood, S., Cox, A. L., Skaguchi, K., Henderson, R. A., Appella, E., Hunt, D. F., Sette, A., and Engelhard, V. Naturally processed peptides longer than nine amino acid residues bind to class I MHC molecule HLA-A2.1 with high affinity and in different conformations. J Immunol 152: 2874-2881, 1994
    • (1994) J Immunol , vol.152 , pp. 2874-2881
    • Chen, Y.1    Sidney, J.2    Southwood, S.3    Cox, A.L.4    Skaguchi, K.5    Henderson, R.A.6    Appella, E.7    Hunt, D.F.8    Sette, A.9    Engelhard, V.10
  • 3
    • 0028150789 scopus 로고
    • Three-dimensional structure of a peptide extending from one end of a class I MHC binding site
    • Collins, E. J., Garboczi, D. N., and Wiley, D. C. Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature 371: 626-629, 1994
    • (1994) Nature , vol.371 , pp. 626-629
    • Collins, E.J.1    Garboczi, D.N.2    Wiley, D.C.3
  • 4
    • 0027370597 scopus 로고
    • HLA-A1 and HLA-A3 T cell epitopes derived from influenza virus proteins predicted from peptide binding motifs
    • DiBrino, M., Tsuchida, T., Turner, R. V., Parker, K. C., Coligan, J. E., and Biddison, W. E. HLA-A1 and HLA-A3 T cell epitopes derived from influenza virus proteins predicted from peptide binding motifs. J Immunol 151: 5930-5935, 1993
    • (1993) J Immunol , vol.151 , pp. 5930-5935
    • DiBrino, M.1    Tsuchida, T.2    Turner, R.V.3    Parker, K.C.4    Coligan, J.E.5    Biddison, W.E.6
  • 5
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk, K., Rötzschke, O., Stevanović, S., Jung, G., and Rammensee, H.-G. Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351: 290-296, 1991
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rötzschke, O.2    Stevanović, S.3    Jung, G.4    Rammensee, H.-G.5
  • 11
    • 0024345149 scopus 로고
    • Specificity pockets for the side chains of peptides antigens in HLA-Aw68
    • Garrett, T. P. J., Saper, M. A., Bjorkman, P. J., Strominger, J. L., and Wiley, D. C. Specificity pockets for the side chains of peptides antigens in HLA-Aw68. Nature 342: 692-696, 1989
    • (1989) Nature , vol.342 , pp. 692-696
    • Garrett, T.P.J.1    Saper, M.A.2    Bjorkman, P.J.3    Strominger, J.L.4    Wiley, D.C.5
  • 12
    • 0026618817 scopus 로고
    • Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle
    • Guo, H.-C., Jardetzky, T. S., Garrett, P. J., Lane, W. S., Strominger, J. L., and Wiley, D. C. Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360: 364-366, 1992
    • (1992) Nature , vol.360 , pp. 364-366
    • Guo, H.-C.1    Jardetzky, T.S.2    Garrett, P.J.3    Lane, W.S.4    Strominger, J.L.5    Wiley, D.C.6
  • 15
    • 0028830185 scopus 로고
    • Grouping HLA-B locus specificities according to shared structural motifs suggests that different peptide-anchoring pockets may have contrasting influence on the course of HIV-1 infection
    • Itescu, S., Rose, S., Dwyer, E., Winchester, R., Grouping HLA-B locus specificities according to shared structural motifs suggests that different peptide-anchoring pockets may have contrasting influence on the course of HIV-1 infection. Hum Immunol 42: 81-89, 1995
    • (1995) Hum Immunol , vol.42 , pp. 81-89
    • Itescu, S.1    Rose, S.2    Dwyer, E.3    Winchester, R.4
  • 18
    • 0022317963 scopus 로고
    • Host resistance directed selectively against H-2 deficient lymphoma variants, analysis of the mechanism
    • Ljunggren, H. G. and Kärre, K. Host resistance directed selectively against H-2 deficient lymphoma variants, analysis of the mechanism. J Exp Med 162: 1745-1759, 1985
    • (1985) J Exp Med , vol.162 , pp. 1745-1759
    • Ljunggren, H.G.1    Kärre, K.2
  • 20
    • 0025813156 scopus 로고
    • The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
    • Madden, D. R., Gorga, J. C., Strominger, J. L., and Wiley, D. C. The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation. Nature 353: 321-325, 1991
    • (1991) Nature , vol.353 , pp. 321-325
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 21
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1Å resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden, D. R., Gorga, J. C., Strominger, J. L., and Wiley, D. C. The three-dimensional structure of HLA-B27 at 2.1Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell 70: 1035-1048, 1992
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 23
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individuals peptide side-chains
    • Parker, K. C., Bednarek, M. A., and Coligan, J. E. Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individuals peptide side-chains. J Immunol 152: 163- 175, 1994
    • (1994) J Immunol , vol.152 , pp. 163-175
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 24
    • 0020040259 scopus 로고
    • A monoclonal antibody directed against the HLA-Bw6 epitope
    • Radka, S. F., Kostyu, D. D., and Amos, D. B. A monoclonal antibody directed against the HLA-Bw6 epitope. J Immunol 128: 2804-2806, 1982
    • (1982) J Immunol , vol.128 , pp. 2804-2806
    • Radka, S.F.1    Kostyu, D.D.2    Amos, D.B.3
  • 27
    • 0028922319 scopus 로고
    • Chemistry of peptides associated with MHC class I and class II molecules
    • Rammensee, H.-G. Chemistry of peptides associated with MHC class I and class II molecules. Curr Opin Immunol 7: 85-96, 1995b
    • (1995) Curr Opin Immunol , vol.7 , pp. 85-96
    • Rammensee, H.-G.1
  • 28
  • 29
    • 0026282918 scopus 로고
    • Susceptibility to subacute thyroiditis is genetically influenced: Familial occurrence in identical twins
    • Rubin, R. A. and Guay, A. J. Susceptibility to subacute thyroiditis is genetically influenced: familial occurrence in identical twins. Thyroid 1: 157-161, 1991
    • (1991) Thyroid , vol.1 , pp. 157-161
    • Rubin, R.A.1    Guay, A.J.2
  • 30
    • 0027304399 scopus 로고
    • Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
    • Ruppert, J., Sidney, J., Celis, E., Kubo, R. T., Gray, H. M. and Sette, A. Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules. Cell 74: 929-937, 1993
    • (1993) Cell , vol.74 , pp. 929-937
    • Ruppert, J.1    Sidney, J.2    Celis, E.3    Kubo, R.T.4    Gray, H.M.5    Sette, A.6
  • 31
    • 0025831493 scopus 로고
    • Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution
    • Saper, M. A., Bjorkman, P. J., and Wiley, D. C. Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution. J Mol Biol 219: 277-319, 1991
    • (1991) J Mol Biol , vol.219 , pp. 277-319
    • Saper, M.A.1    Bjorkman, P.J.2    Wiley, D.C.3
  • 34
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith, K. J., Reid, S. W., Stuart, D. I., McMichael, A. J., Jones, E. Y., and Bell, J. I. An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4: 203-213, 1996
    • (1996) Immunity , vol.4 , pp. 203-213
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 37
    • 0029974607 scopus 로고    scopus 로고
    • Immunogenicity of peptides bound to MHC class I molecules depends on the MHC-peptide complex stability
    • Van der Burg, S. H., Visseren, M. J. W., Brandt, R. M. P., Kast, W. M., and Melief, C. J. M. Immunogenicity of peptides bound to MHC class I molecules depends on the MHC-peptide complex stability. J Immunol 156: 3308-3314, 1996
    • (1996) J Immunol , vol.156 , pp. 3308-3314
    • Van Der Burg, S.H.1    Visseren, M.J.W.2    Brandt, R.M.P.3    Kast, W.M.4    Melief, C.J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.