Peptide sequences binding to MHC class I proteins

Margaret H. Smith, Kit S. Lam, Evan M. Hersh, Michal Lebl, William J. Grimes

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Motifs for peptides which bind specifically to the human class I major histocompatibility complex molecules HLA-A2 and B7 were determined by sequence analysis of class I-bound peptides selected from a random synthetic library of nonamers. Thirteen individual peptides were sequenced for HLA-A2, twelve individual and nine pooled peptides were sequenced for HLA-B7. Analysis of sequence alignment implicated four peptide positions in potential contact with the class I HLA-A2 molecule and three positions for the HLA-B7 molecule. The results demonstrate that a synthetic peptide library can be used to identify allele-specific motifs for class I molecules, providing information comparable to the results obtained from sequencing endogenous peptides. This method utilizes denatured class I heavy chains, and similar results were obtained using a class I protein purified from mammalian cells or by expression in Escherichia coli. This method has the potential to detect peptides which may not be generated physiologically, but due to their binding properties, may be valuable to predict or engineer immunomodulatory T cell epitopes.

Original languageEnglish (US)
Pages (from-to)1431-1437
Number of pages7
JournalMolecular Immunology
Issue number18
StatePublished - Dec 1994


  • T-cell
  • antigens
  • major histocompatibility
  • peptides

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology


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