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

Lars Kjer-Nielsen, Craig S. Clements, Andrew G. Brooks, Anthony W. Purcell, James McCluskey, Jamie Rossjohn

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65 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1521-1532
Number of pages12
Issue number11
Publication statusPublished - 1 Nov 2002


  • Crystal structure
  • Epstein-Barr virus
  • Immunity
  • Immuno-dominance
  • Public
  • T cell receptor

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