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

被引：0
作者：
Fleur E Tynan
Hugh H Reid
Lars Kjer-Nielsen
John J Miles
Matthew C J Wilce
Lyudmila Kostenko
Natalie A Borg
Nicholas A Williamson
Travis Beddoe
Anthony W Purcell
Scott R Burrows
James McCluskey
Jamie Rossjohn
机构：
[1] The Protein Crystallography Unit,Department of Biochemistry and Molecular Biology
[2] School of Biomedical Sciences,Department of Microbiology & Immunology
[3] Monash University,Department of Biochemistry
[4] University of Melbourne,undefined
[5] Cellular Immunology Laboratory,undefined
[6] Queensland Institute of Medical Research,undefined
[7] University of Melbourne,undefined
来源：
Nature Immunology | 2007年 / 8卷
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摘要：
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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页码：268 / 276
页数：8
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