A functional hot spot for antigen recognition in a superagonist TCR/MHC complex

Massimo Degano, K. Christopher Garcia, Vasso Apostolopoulos, Markus G. Rudolph, Luc Teyton, Ian A. Wilson

Research output: Contribution to journalArticlepeer-review

Abstract

A longstanding question in T cell receptor signaling is how structurally similar ligands, with similar affinities, can have substantially different biological activity. The crystal structure of the 2C TCR complex of H-2Kb with superagonist peptide SlYR at 2.8 Å elucidates a structural basis for TCR discrimination of altered peptide ligands. The difference in antigen potency is modulated by two cavities in the TCR combining site, formed mainly by CDRs 3α, 3β, and 1β, that complement centrally located peptide residues. This 'functional hot spot' allows the TCR to finely discriminate amongst energetically similar interactions within different ligands for those in which the peptide appropriately stabilizes the TCR/pMHC complex and provides a new structural perspective for understanding differential signaling resulting from T cell cross-reactivity.

Original languageEnglish
Pages (from-to)251-261
Number of pages11
JournalImmunity
Volume12
Issue number3
Publication statusPublished - 2000

ASJC Scopus subject areas

  • Immunology and Allergy
  • Infectious Diseases
  • Immunology

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