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 peptides1,2. 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 motifs3. We have previously reported an analysis of MHC class II-associated peptide sequences4. 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.
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Rudensky, A., Preston-Hurlburt,, P., Al-Ramadi, B. et al. Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs. Nature 359, 429–431 (1992). https://doi.org/10.1038/359429a0
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DOI: https://doi.org/10.1038/359429a0
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