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Immunogenetics

, Volume 39, Issue 1, pp 74–77 | Cite as

Dominant aromatic/aliphatic C-terminal anchor in HLA-B*2702 and B*2705 peptide motifs

  • Olaf Rötzschke
  • Kirsten Falk
  • Stefan Stevanovic
  • Volker Gnau
  • Günther Jung
  • Hans-Georg Rammensee
MHC Peptide Motif Register

Keywords

Peptide Peptide Motif 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Barnstable, C. J., Bodmer, W. F., Brown, G., Galfre, G., Milstein, C., Williams, A. F., and Ziegler, A. Production of monoclonal antibodies in group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis. Cell 14: 9–20, 1978Google Scholar
  2. Bjorkman, P. J. and Parham, P. Structure, function, and diversity of class I major histocompatibility complex molecules. Annu Rev Biochem 59: 253–288, 1990Google Scholar
  3. 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, 1991CrossRefPubMedGoogle Scholar
  4. Falk, K., Rötzschke, O., Faath, S., Goth, S., Graef, I., Shastri, N., and Rammensee, H.-G. Both human and mouse cells expressing H-2Kb and ovalbumin process the same peptide, SIINFEKL. Cell Immunol 150, in press, 1993Google Scholar
  5. Jardetzky, T. S., Lane, W. S., Robinson, R. A., Madden, D. R., and Wiley, D. C. Identification of self peptides bound to purified HLA-B27. Nature 353: 326–329, 1991Google Scholar
  6. 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, 1991Google Scholar
  7. Matsamura, M., Fremont, D. H., Peterson, P., and Wilson, I. A. Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257: 927–934, 1992Google Scholar
  8. Parham, P. and Bodmer, W. F. Monoclonal antibodyto a human histocompatibility alloantigen, HLA-A2. Nature 276: 397–399, 1978Google Scholar
  9. Parham, P. and Brodsky, F. M. Partial purification and some properties of BB7.2. Hum Immunol 3: 277–299, 1981Google Scholar
  10. Rötzschke, O., Falk, K., Stevanovic S., Jung, G., and Rammensee, H.-G. Peptide motifs of closely related HLA class I molecules encompass substantial differences. Eur J Immunol 22: 2453–2456, 1992Google Scholar
  11. Thurau, S. R., Wildner, G., Kuon, W., Weiss, E. H., and Riethmüller, G. Expression and immunogenicity of HLA-B27 in high-transfection recipient P815: a new method to induce monoclonal antibodies directed against HLA-B27. Tissue Antigens 33: 511–519, 1989Google Scholar

Copyright information

© Springer-Verlag 1994

Authors and Affiliations

  • Olaf Rötzschke
    • 1
  • Kirsten Falk
    • 1
  • Stefan Stevanovic
    • 2
  • Volker Gnau
    • 2
  • Günther Jung
    • 2
  • Hans-Georg Rammensee
    • 1
  1. 1.Max-Planck-Institut für BiologieAbteilung ImmungenetikTübingenGermany
  2. 2.Institut für Organische ChemieUniversität TübingenTübingenGermany

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