2nw3: Difference between revisions
New page: left|200px<br /> <applet load="2nw3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nw3, resolution 1.700Å" /> '''Crystal structure ... |
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[[Image:2nw3.gif|left|200px]]<br /> | [[Image:2nw3.gif|left|200px]]<br /><applet load="2nw3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2nw3, resolution 1.700Å" /> | caption="2nw3, resolution 1.700Å" /> | ||
'''Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A'''<br /> | '''Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A'''<br /> | ||
==Overview== | ==Overview== | ||
Plasticity of the T cell receptor (TCR) is a hallmark of major | 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== | ||
2NW3 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:// | 2NW3 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=2NW3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Reid, H | [[Category: Reid, H H.]] | ||
[[Category: Rossjohn, J.]] | [[Category: Rossjohn, J.]] | ||
[[Category: Tynan, F | [[Category: Tynan, F E.]] | ||
[[Category: hla-b*3508]] | [[Category: hla-b*3508]] | ||
[[Category: mhc]] | [[Category: mhc]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:45 2008'' | ||
Revision as of 19:11, 21 February 2008
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Crystal structure of HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A
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.
DiseaseDisease
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 StructureAbout this Structure
2NW3 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
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