Article abstract
Nature Immunology 8, 268 - 276 (2007)
Published online: 28 January 2007 | doi:10.1038/ni1432
A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule
Fleur E Tynan1,5, Hugh H Reid1,5, Lars Kjer-Nielsen2, John J Miles3, Matthew C J Wilce1, Lyudmila Kostenko2, Natalie A Borg1, Nicholas A Williamson4, Travis Beddoe1, Anthony W Purcell4, Scott R Burrows3, James McCluskey2 & Jamie Rossjohn1
Abstract
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.
- The Protein Crystallography Unit, Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Victoria 3800, Australia.
- Department of Microbiology & Immunology, University of Melbourne, Parkville, Victoria 3010, Australia.
- Cellular Immunology Laboratory, Queensland Institute of Medical Research, Brisbane, 4029, Australia.
- Department of Biochemistry, University of Melbourne, Parkville, Victoria 3010, Australia.
- These authors contributed equally to this work.
Correspondence to: James McCluskey2 e-mail: jamesm1@unimelb.edu.au
Correspondence to: Jamie Rossjohn1 e-mail: jamie.rossjohn@med.monash.edu.au
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