Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs

Alexander Yu Rudensky, Paula Preston-Hurlburt, Basel K. Al-Ramadi, Jonathan Rothbard, Charles A. Janeway

Research output: Contribution to journalArticlepeer-review

248 Citations (Scopus)


T cells recognize foreign protein antigens in the form of peptide fragments bound tightly to the outer aspect of molecules encoded by the major histocompatibility complex (MHC). Most of the amino-acid differences that distinguish MHC allelic variants line the peptide-binding cleft, and different allelic forms of MHC molecules bind distinct peptides It has been demonstrated that peptide-binding to MHC class I involves anchor residues in certain positions and that antigenic peptides associated with MHC class I exhibit allele-specific structural motifs We have previously reported an analysis of MHC class II-associated peptide sequences Here we extend this analysis and show that certain amino-acid residues occur at particular positions in the sequence of peptides binding to a given MHC class II molecule. These sequence motifs require the amino terminus to be shifted one or two positions to obtain alignment; such shifts occur naturally for a single peptide sequence without qualitatively altering CD4 T-cell recognition.

Original languageEnglish
Pages (from-to)429-431
Number of pages3
Issue number6394
Publication statusPublished - 1992
Externally publishedYes

ASJC Scopus subject areas

  • General


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