2nw2: Difference between revisions

Revision as of 22:46, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nw2.png

Template:STRUCTURE 2nw2

Crystal structure of ELS4 TCR at 1.4ACrystal structure of ELS4 TCR at 1.4A

Template:ABSTRACT PUBMED 17259989

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule., Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, Borg NA, Williamson NA, Beddoe T, Purcell AW, Burrows SR, McCluskey J, Rossjohn J, Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:17259989

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OCA

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-'''Crystal structure of ELS4 TCR at 1.4A'''
+===Crystal structure of ELS4 TCR at 1.4A===
-==Overview==
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-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 line below this paragraph, {{ABSTRACT_PUBMED_17259989}}, adds the Publication Abstract to the page
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 [[Category: Tynan, F E.]]
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