4z7u: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z7u]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z7U FirstGlance]. <br> | <table><tr><td colspan='2'>[[4z7u]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z7U FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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]] 2.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</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'>[https://proteopedia.org/fgij/fg.htm?mol=4z7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z7u OCA], [https://pdbe.org/4z7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z7u RCSB], [https://www.ebi.ac.uk/pdbsum/4z7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z7u 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=4z7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z7u OCA], [https://pdbe.org/4z7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z7u RCSB], [https://www.ebi.ac.uk/pdbsum/4z7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z7u ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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==See Also== | ==See Also== | ||
*[[Gluten|Gluten]] | *[[Gluten|Gluten]] | ||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC II 3D structures|MHC II 3D structures]] | |||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | ||
== References == | == References == | ||
Revision as of 11:13, 27 September 2023
S13 complexS13 complex
Structural highlights
FunctionGDA9_WHEAT Gliadin is the major seed storage protein in wheat. Publication Abstract from PubMedIn HLA-DQ8-associated celiac disease (CD), the pathogenic T cell response is directed toward an immunodominant alpha-gliadin-derived peptide (DQ8-glia-alpha1). However, our knowledge of TCR gene usage within the primary intestinal tissue of HLA-DQ8+ CD patients is limited. We identified two populations of HLA-DQ8-glia-alpha1 tetramer+ CD4+ T cells that were essentially undetectable in biopsy samples from patients on a gluten-free diet but expanded rapidly and specifically after antigenic stimulation. Distinguished by expression of TRBV9, both T cell populations displayed biased clonotypic repertoires and reacted similarly against HLA-DQ8-glia-alpha1. In particular, TRBV9 paired most often with TRAV26-2, whereas the majority of TRBV9- TCRs used TRBV6-1 with no clear TRAV gene preference. Strikingly, both tetramer+/TRBV9+ and tetramer+/TRBV9- T cells possessed a non-germline-encoded arginine residue in their CDR3alpha and CDR3beta loops, respectively. Comparison of the crystal structures of three TRBV9+ TCRs and a TRBV9- TCR revealed that, as a result of distinct TCR docking modes, the HLA-DQ8-glia-alpha1 contacts mediated by the CDR3-encoded arginine were almost identical between TRBV9+ and TRBV9- TCRs. In all cases, this interaction centered on two hydrogen bonds with a specific serine residue in the bound peptide. Replacement of serine with alanine at this position abrogated TRBV9+ and TRBV9- clonal T cell proliferation in response to HLA-DQ8-glia-alpha1. Gluten-specific memory CD4+ T cells with structurally and functionally conserved TCRs therefore predominate in the disease-affected tissue of patients with HLA-DQ8-mediated CD. Determinants of Gliadin-Specific T Cell Selection in Celiac Disease.,Petersen J, van Bergen J, Loh KL, Kooy-Winkelaar Y, Beringer DX, Thompson A, Bakker SF, Mulder CJ, Ladell K, McLaren JE, Price DA, Rossjohn J, Reid HH, Koning F J Immunol. 2015 May 6. pii: 1500161. PMID:25948817[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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