Structural analysis of mhc class i molecules with bound peptide antigens

Ian A. Wilson, Daved H. Fremont

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Three-dimensional structures of human and murine MHC class I molecules in complex with peptide antigens have begun to elucidate the mechanism of peptide binding. The MHC molecule has a highly conserved structure in which important variation occurs only in the residues lining the central polymorphic portion of the peptide binding cleft. Peptides bind in extended conformations deep within the cleft and have highly specific and conserved interactions at their amino and carboxyl termini and divergent interactions in the middle. Peptides longer than the canonical length for a given allele appear to bulge in the middle but maintain their interactions at their ends. One or more anchor residues are used by the peptide to establish tight and enduring presentation to T cells, Peptide-associated conformational differences in the MHC molecule itself may contribute to the T cell recognition process.

Original languageEnglish
Pages (from-to)75-80
Number of pages6
JournalSeminars in immunology
Volume5
Issue number2
DOIs
StatePublished - Apr 1993

Keywords

  • Conformational changes
  • MHC class I structure
  • MHC specificity
  • Peptide binding
  • T cell recognition

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