2nw2: Difference between revisions

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-[[Image:2nw2.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2nw2", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2nw2|  PDB=2nw2  |  SCENE=  }}
-'''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]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</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>
+== Function ==
+[https://www.uniprot.org/uniprot/Q6P4G7_HUMAN Q6P4G7_HUMAN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nw/2nw2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nw2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Overview==
+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<ref>PMID:17259989</ref>
-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==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NW2 OCA].
+</div>
+<div class="pdbe-citations 2nw2" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/17259989 17259989]
+*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
-[[Category: Reid, H H.]]
+== References ==
-[[Category: Rossjohn, J.]]
+<references/>
-[[Category: Tynan, F E.]]
+__TOC__
-[[Category: T cell receptor]]
+</StructureSection>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:58:43 2008''
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Reid HH]]
+[[Category: Rossjohn J]]
+[[Category: Tynan FE]]