6xqq
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6xqq is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of human D462-E4 TCR== | |
| + | <StructureSection load='6xqq' size='340' side='right'caption='[[6xqq]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6xqq]] is a 4 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=6XQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XQQ 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]] 2.68Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6xqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xqq OCA], [https://pdbe.org/6xqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xqq RCSB], [https://www.ebi.ac.uk/pdbsum/6xqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xqq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | MR1 presents vitamin B-related metabolites to mucosal associated invariant T (MAIT) cells, which are characterized, in part, by the TRAV1-2(+) alphabeta T cell receptor (TCR). In addition, a more diverse TRAV1-2(-) MR1-restricted T cell repertoire exists that can possess altered specificity for MR1 antigens. However, the molecular basis of how such TRAV1-2(-) TCRs interact with MR1-antigen complexes remains unclear. Here, we describe how a TRAV12-2(+) TCR (termed D462-E4) recognizes an MR1-antigen complex. We report the crystal structures of the unliganded D462-E4 TCR and its complex with MR1 presenting the riboflavin-based antigen 5-OP-RU. Here, the TRBV29-1 beta-chain of the D462-E4 TCR binds over the F'-pocket of MR1, whereby the complementarity-determining region (CDR) 3beta loop surrounded and projected into the F'-pocket. Nevertheless, the CDR3beta loop anchored proximal to the MR1 A'-pocket and mediated direct contact with the 5-OP-RU antigen. The D462-E4 TCR footprint on MR1 contrasted that of the TRAV1-2(+) and TRAV36(+) TCRs' docking topologies on MR1. Accordingly, diverse MR1-restricted T cell repertoire reveals differential docking modalities on MR1, thus providing greater scope for differing antigen specificities. | ||
| - | + | Atypical TRAV1-2(-) T cell receptor recognition of the antigen-presenting molecule MR1.,Awad W, Meermeier EW, Sandoval-Romero ML, Le Nours J, Worley AH, Null MD, Liu L, McCluskey J, Fairlie DP, Lewinsohn DM, Rossjohn J J Biol Chem. 2020 Oct 16;295(42):14445-14457. doi: 10.1074/jbc.RA120.015292. Epub, 2020 Aug 14. PMID:32817339<ref>PMID:32817339</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6xqq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Awad W]] | ||
| + | [[Category: Rossjohn J]] | ||
Current revision
Structure of human D462-E4 TCR
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