Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition

Jeffrey A. Bluestone*, Stephen Jameson, Stephen Miller, Robert Dick

*Corresponding author for this work

Research output: Contribution to journalArticle

125 Scopus citations

Abstract

Small peptides, derived from endogenous proteins bind within the antigen binding groove created by the β-pleated sheets and α helices of the α1 and α2 domains of the class I molecule of the major histocompatibility complex (MHC). However, the precise role of peptide in class I MHC conformation remains unclear. Here, we have shown that, in at least some instances, changes induced in the MHC molecule by the binding of distinct peptides can be identified as specific alterations in serological epitopes expressed on the class I protein. The nature of specific peptides expressed by dass I-bearing cells may, therefore, have a dramatic influence on T cell development, self-tolerance, and alloreactivity.

Original languageEnglish (US)
Pages (from-to)1757-1761
Number of pages5
JournalJournal of Experimental Medicine
Volume176
Issue number6
DOIs
StatePublished - Dec 1 1992

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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