The 1.5 Å crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance

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Abstract

Despite a potential repertoire of >1015 αβ T cell receptors (TcR), the HLA B8-restricted cytolytic T cell response to a latent antigen of Epstein-Barr virus (EBV) is strikingly limited in the TcR sequences that are selected. Even in unrelated individuals this response is dominated by a single highly restricted TcR clonotype that selects identical combinations of hypervariable Vα, Vβ, D, J, and N region genes. We have determined the 1.5 Å crystal structure of this "public" TcR, revealing that five of the six hypervariable loops adopt novel conformations providing a unique combining site that contains a deep pocket predicted to overlay the HLA B8-peptide complex. The findings suggest a structural basis for the immunodominance of this clonotype in the immune response to EBV.

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Kjer-Nielsen, L., Clements, C. S., Brooks, A. G., Purcell, A. W., McCluskey, J., & Rossjohn, J. (2002). The 1.5 Å crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance. Structure, 10(11), 1521–1532. https://doi.org/10.1016/S0969-2126(02)00878-X

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