A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule

Fleur Elizabeth Tynan, Hugh Harrington Reid, Lars Kjer-Nielsen, John J Miles, Matthew Charles James Wilce, Lyudmila Kostenko, Natalie Borg, Nicholas A Williamson, Travis Clarke Beddoe, Anthony W Purcell, S R Burrows, James McCluskey, Jamie Rossjohn

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181 Citations (Scopus)


Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent bulged Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide bulldozing created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.
Original languageEnglish
Pages (from-to)268 - 276
Number of pages9
JournalNature Immunology
Issue number3
Publication statusPublished - 2007

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