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., McCluskey, James, and Rossjohn, Jamie (2007) A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nature Immunology, 8 (3). pp. 268-276.

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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.

Item ID:	45396
Item Type:	Article (Research - C1)
ISSN:	1529-2916
Funders:	Australian Research Council (ARC), National Health and Medical Research Council (NHMRC), Roche Organ Transplant Research Fund (ROTRF)
Date Deposited:	07 Sep 2016 01:57
FoR Codes:	11 MEDICAL AND HEALTH SCIENCES > 1107 Immunology > 110702 Applied Immunology (incl Antibody Engineering, Xenotransplantation and T-cell Therapies) @ 100%
SEO Codes:	92 HEALTH > 9201 Clinical Health (Organs, Diseases and Abnormal Conditions) > 920108 Immune System and Allergy @ 100%
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