Structures of an MHC class II molecule with covalently bound single peptides

Daved H. Fremont, Wayne A. Hendrickson, Philippa Marrack, John Kappler

Research output: Contribution to journalArticle

328 Scopus citations

Abstract

The high-resolution x-ray crystal structures of the murine major histocompatibility complex (MHC) class II molecule, I-E(k), occupied by either of two antigenic peptides were determined. They reveal the structural basis for the I-E(k) peptide binding motif and suggest general principles for additional alleles. A buried cluster of acidic amino acids in the binding groove predicted to be conserved among all murine I-E and human DR MHC class II molecules suggests how pH may influence MHC binding or exchange of peptides. These structures also complement mutational studies on the importance of individual peptide residues to T cell receptor recognition.

Original languageEnglish
Pages (from-to)1001-1004
Number of pages4
JournalScience
Volume272
Issue number5264
DOIs
StatePublished - May 17 1996
Externally publishedYes

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