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• W2089004428 endingPage "13284" @default.
• W2089004428 startingPage "13279" @default.
• W2089004428 abstract "T cells generally recognize peptide antigens bound to MHC proteins through contacts with residues found within or immediately flanking the seven- to nine-residue sequence accommodated in the MHC peptide-binding groove. However, some T cells require peptide residues outside this region for activation, the structural basis for which is unknown. Here, we have investigated a HIV Gag-specific T cell clone that requires an unusually long peptide antigen for activation. The crystal structure of a minimally antigenic 16-mer bound to HLA-DR1 shows that the peptide C-terminal region bends sharply into a hairpin turn as it exits the binding site, orienting peptide residues outside the MHC-binding region in position to interact with a T cell receptor. Peptide truncation and substitution studies show that both the hairpin turn and the extreme C-terminal residues are required for T cell activation. These results demonstrate a previously unrecognized mode of MHC-peptide-T cell receptor interaction." @default.
• W2089004428 created "2016-06-24" @default.
• W2089004428 creator A5016518899 @default.
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• W2089004428 creator A5051080788 @default.
• W2089004428 creator A5054495834 @default.
• W2089004428 creator A5065542402 @default.
• W2089004428 date "2004-08-26" @default.
• W2089004428 modified "2023-10-01" @default.
• W2089004428 title "A hairpin turn in a class II MHC-bound peptide orients residues outside the binding groove for T cell recognition" @default.
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• W2089004428 doi "https://doi.org/10.1073/pnas.0403371101" @default.
• W2089004428 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/516560" @default.
• W2089004428 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15331779" @default.
• W2089004428 hasPublicationYear "2004" @default.
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