Abstract
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 language | English |
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Pages (from-to) | 429-431 |
Number of pages | 3 |
Journal | Nature |
Volume | 359 |
Issue number | 6394 |
DOIs | |
Publication status | Published - Jan 1 1992 |
Externally published | Yes |
ASJC Scopus subject areas
- General