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- W2275997631 abstract "Significance T-cell receptor (TCR) recognition of antigenic peptides presented by major histocompatibility complex (MHC) proteins defines specificity in cellular immunity. Evidence suggests that TCRs are intrinsically biased toward MHC proteins, yet how this bias coexists alongside the considerable structural variability that is necessary for TCRs to engage different ligands has been a longstanding puzzle. By examining structural and sequence data, we found evidence that human αβ TCRs have an inherent compatibility with structural and chemical properties of MHC proteins. This compatibility leads TCRs to an intrinsic MHC bias but does not compel the formation of particular modes of binding, providing a solution to how TCRs can be MHC-biased but still structurally adaptable." @default.
- W2275997631 created "2016-06-24" @default.
- W2275997631 creator A5017774638 @default.
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- W2275997631 date "2016-02-16" @default.
- W2275997631 modified "2023-10-01" @default.
- W2275997631 title "How structural adaptability exists alongside HLA-A2 bias in the human αβ TCR repertoire" @default.
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- W2275997631 doi "https://doi.org/10.1073/pnas.1522069113" @default.
- W2275997631 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4780628" @default.