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

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...

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Bibliographic Details
Published inNature Immunology Vol. 8; no. 3; pp. 268 - 276
Main Authors McCluskey, James, Rossjohn, Jamie, Tynan, Fleur E, Reid, Hugh H, Kjer-Nielsen, Lars, Miles, John J, Wilce, Matthew C J, Kostenko, Lyudmila, Borg, Natalie A, Williamson, Nicholas A, Beddoe, Travis, Purcell, Anthony W, Burrows, Scott R
Format Journal Article
LanguageEnglish
Published United States Nature Publishing Group 01.03.2007
Subjects
Animals
Antigen Presentation - immunology
Antigens, Viral - chemistry
Antigens, Viral - immunology
Cell receptors
Epitopes, T-Lymphocyte - chemistry
Epitopes, T-Lymphocyte - immunology
Epstein-Barr virus
Flow Cytometry
Histocompatibility Antigens Class I - chemistry
Histocompatibility Antigens Class I - immunology
Humans
Immune recognition
Major histocompatibility complex
Physiological aspects
Plasticity
Protein Structure, Quaternary
Receptors, Antigen, T-Cell - chemistry
Receptors, Antigen, T-Cell - immunology
T cells
Australia
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Summary: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.
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ISSN:1529-2908
1529-2916
1365-2567
DOI:10.1038/ni1432