5ks9: Difference between revisions

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'''Unreleased structure'''


The entry 5ks9 is ON HOLD  until Paper Publication
==Bel502-DQ8-glia-alpha1 complex==
<StructureSection load='5ks9' size='340' side='right' caption='[[5ks9]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ks9]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KS9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KS9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5ks9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ks9 OCA], [http://pdbe.org/5ks9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ks9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ks9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ks9 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In HLA-DQ8-associated celiac disease, TRAV26-2+-TRBV9+ and TRAV8-3+-TRBV6+ T cells recognize the immunodominant DQ8-glia-alpha1 epitope, whereupon a non-germline-encoded arginine residue played a key role in binding HLA-DQ8-glia-alpha1. Whether distinct T cell receptor (TCR) recognition modes exist for gliadin epitopes remains unclear. TCR repertoire analysis revealed populations of HLA-DQ8-glia-alpha1 and HLA-DQ8.5-glia-gamma1 restricted TRAV20+-TRBV9+ T cells that did not possess a non-germline-encoded arginine residue. The crystal structures of a TRAV20+-TRBV9+ TCR-HLA-DQ8-glia-alpha1 complex and two TRAV20+-TRBV9+ TCR-HLA-DQ8.5-glia-gamma1 complexes were determined. This revealed that the differential specificity toward DQ8-glia-alpha1 and DQ8.5-glia-gamma1 was governed by CDR3beta-loop-mediated interactions. Surprisingly, a germline-encoded arginine residue within the CDR1alpha loop of the TRAV20+ TCR substituted for the role of the non-germline-encoded arginine in the TRAV26-2+-TRBV9+ and TRAV8-3+-TRBV6+ TCRs. Thus, in celiac disease, the responding TCR repertoire is driven by a common mechanism that selects for structural elements within the TCR that have convergent binding solutions in HLA-DQ8-gliadin recognition.


Authors:  
Diverse T Cell Receptor Gene Usage in HLA-DQ8-Associated Celiac Disease Converges into a Consensus Binding Solution.,Petersen J, Kooy-Winkelaar Y, Loh KL, Tran M, van Bergen J, Koning F, Rossjohn J, Reid HH Structure. 2016 Aug 23. pii: S0969-2126(16)30221-0. doi:, 10.1016/j.str.2016.07.010. PMID:27568928<ref>PMID:27568928</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5ks9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Petersen, J]]
[[Category: Reid, H H]]
[[Category: Rossjohn, J]]
[[Category: Celiac disease t cell receptor peptide mhc complex]]
[[Category: Immune system]]
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