A region of conformational variability outside the peptide-binding site of a class I MHC molecule

Scott T. Kuhns, Larry R. Pease

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Peptide binding is known to influence the conformation of the surface of class I molecules as detected with mAbs and TCR. A new conformationally sensitive epitope on the mouse class I molecule Kb is defined by mAb AF6- 88.5. The recognized structure is affected by amino acid substitutions in any of the three external domains of the class I heavy chain and, in addition, is influenced by the substitution of human for mouse β2-microglobulin. Interestingly, the epitope for this Ab is not affected by mutations within the peptide-binding cleft or by the nature of the peptide bound. These findings indicate that the effect of a change in one domain of class I can radiate to other parts of the molecule. Furthermore, the existence of conformationally sensitive structures outside of the peptide-binding site suggests the possibility that class I molecules may change their structure in response to binding by receptors and ligands such as the TCR and the coligand CD8. Such structural changes may represent signals that can influence cellular activation events.

Original languageEnglish (US)
Pages (from-to)6745-6750
Number of pages6
JournalJournal of Immunology
Volume161
Issue number12
StatePublished - Dec 15 1998

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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