The lack of consensus for I-Ag7-peptide binding motifs: Is there a requirement for anchor amino acid side chains?

Eugenio Carrasco-Marin, Osami Kanagawa, Emil R. Unanue

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

We discuss here the problems in identifying sequence motifs of peptides that bind to I-Ag7, the class II histocompatibility molecule of NOD diabetic mice. We present studies that indicate a minor contribution of amino acid side chains for binding. A peptide from the Eα chain binds to I-Ag7 molecules and is recognized by CD4 T cells. By producing single-residue mutations we identified four residues that were considered to contact the T cell receptor. No residue was found to be essential for binding to I-Ag7: a peptide that contained the T cell contact residues, on a backbone of alanines, bound to I-Ag7 and stimulated the T cells. We conclude that peptides can bind to I-Ag7 without the requirement for residues with prominent side chains to anchor them.

Original languageEnglish
Pages (from-to)8621-8626
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number15
StatePublished - Jul 20 1999

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