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2nx5

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(New page: 200px<br /> <applet load="2nx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nx5, resolution 2.700&Aring;" /> '''Crystal structure ...)
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[[Image:2nx5.gif|left|200px]]<br />
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[[Image:2nx5.gif|left|200px]]<br /><applet load="2nx5" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2nx5" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2nx5, resolution 2.700&Aring;" />
caption="2nx5, resolution 2.700&Aring;" />
'''Crystal structure of ELS4 TCR bound to HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A'''<br />
'''Crystal structure of ELS4 TCR bound to HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A'''<br />
==Overview==
==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.
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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2NX5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NX5 OCA].
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2NX5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NX5 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Reid, H.H.]]
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[[Category: Reid, H H.]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
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[[Category: Tynan, F.E.]]
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[[Category: Tynan, F E.]]
[[Category: immune complex]]
[[Category: immune complex]]
[[Category: tcr-pmhc]]
[[Category: tcr-pmhc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:03:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:58 2008''

Revision as of 16:11, 21 February 2008


2nx5, resolution 2.700Å

Drag the structure with the mouse to rotate

Crystal structure of ELS4 TCR bound to HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A

Contents

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.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]

About this Structure

2NX5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 18:11:58 2008

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