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| | ==Crystal structure of ELS4 TCR at 1.4A== | | ==Crystal structure of ELS4 TCR at 1.4A== |
| - | <StructureSection load='2nw2' size='340' side='right' caption='[[2nw2]], [[Resolution|resolution]] 1.40Å' scene=''> | + | <StructureSection load='2nw2' size='340' side='right'caption='[[2nw2]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nw2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NW2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NW2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nw3|2nw3]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nw2 OCA], [http://pdbe.org/2nw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nw2 RCSB], [http://www.ebi.ac.uk/pdbsum/2nw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nw2 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nw2 OCA], [https://pdbe.org/2nw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nw2 RCSB], [https://www.ebi.ac.uk/pdbsum/2nw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nw2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6P4G7_HUMAN Q6P4G7_HUMAN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[T-cell receptor|T-cell receptor]] | + | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Reid, H H]] | + | [[Category: Large Structures]] |
| - | [[Category: Rossjohn, J]] | + | [[Category: Reid HH]] |
| - | [[Category: Tynan, F E]] | + | [[Category: Rossjohn J]] |
| - | [[Category: Immune system]] | + | [[Category: Tynan FE]] |
| - | [[Category: T cell receptor]]
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| Structural highlights
Function
Q6P4G7_HUMAN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:17259989 doi:10.1038/ni1432
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