2nw2: Difference between revisions

Revision as of 19:11, 21 February 2008

Crystal structure of ELS4 TCR at 1.4A

OverviewOverview

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.

About this StructureAbout this Structure

2NW2 is a Protein complex structure of sequences from Homo sapiens. 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

Page seeded by OCA on Thu Feb 21 18:11:37 2008

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Reid, H.H.]]
+[[Category: Reid, H H.]]
 [[Category: Rossjohn, J.]]
-[[Category: Tynan, F.E.]]
+[[Category: Tynan, F E.]]
 [[Category: t cell receptor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:00:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:37 2008''