Delineation of antigen contact residues on an MHC class II molecule

Jean Peccoud, Paolo Dellabona, Paul Allen, Christophe Benoist, Diane Mathis

Research output: Contribution to journalArticle

Abstract

This report describes a detailed mutational analysis of a major histocompatibility complex class II moleculethe a chain of the Ak complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of Ak by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.

Original languageEnglish
Pages (from-to)4215-4223
Number of pages9
JournalEMBO Journal
Volume9
Issue number13
Publication statusPublished - 1990

Keywords

  • Antigen presentation
  • Major histocompatibility complex
  • Site-specific mutagenesis
  • T cell recognition

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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  • Cite this

    Peccoud, J., Dellabona, P., Allen, P., Benoist, C., & Mathis, D. (1990). Delineation of antigen contact residues on an MHC class II molecule. EMBO Journal, 9(13), 4215-4223.