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• W2788442932 abstract "Abstract Human leukocyte antigen (HLA)-I molecules generally bind short peptides (8–10 amino acids), although extended HLA-I restricted peptides (>10 amino acids) can be presented to T cells. However, the function of such extended HLA-I epitopes in tumour immunity, and how they would be recognised by T-cell receptors (TCR) remains unclear. Here we show that the structures of two distinct TCRs (TRAV4 + TRAJ21 + -TRBV28 + TRBJ2-3 + and TRAV4 + TRAJ8 + -TRBV9 + TRBJ2 - 1 + ), originating from a polyclonal T-cell repertoire, bind to HLA-B*07:02, presenting a 13-amino-acid-long tumour-associated peptide, NY-ESO-1 60–72 . Comparison of the structures reveals that the two TCRs differentially binds NY-ESO-1 60–72 –HLA-B*07:02 complex, and induces differing extent of conformational change of the NY-ESO-1 60–72 epitope. Accordingly, polyclonal TCR usage towards an extended HLA-I restricted tumour epitope translates to differing TCR recognition modes, whereby extensive flexibility at the TCR–pHLA-I interface engenders recognition." @default.
• W2788442932 created "2018-03-06" @default.
• W2788442932 creator A5017677707 @default.
• W2788442932 creator A5023421955 @default.
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• W2788442932 date "2018-03-12" @default.
• W2788442932 modified "2023-10-14" @default.
• W2788442932 title "Divergent T-cell receptor recognition modes of a HLA-I restricted extended tumour-associated peptide" @default.
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• W2788442932 doi "https://doi.org/10.1038/s41467-018-03321-w" @default.
• W2788442932 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5847591" @default.
• W2788442932 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29531227" @default.
• W2788442932 hasPublicationYear "2018" @default.
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