4grl: Difference between revisions
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==Crystal structure of a autoimmune TCR-MHC complex== | ==Crystal structure of a autoimmune TCR-MHC complex== | ||
<StructureSection load='4grl' size='340' side='right' caption='[[4grl]], [[Resolution|resolution]] 2.86Å' scene=''> | <StructureSection load='4grl' size='340' side='right'caption='[[4grl]], [[Resolution|resolution]] 2.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4grl]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4grl]] 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=4GRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GRL FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.86Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4grl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4grl OCA], [https://pdbe.org/4grl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4grl RCSB], [https://www.ebi.ac.uk/pdbsum/4grl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4grl ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q30066_HUMAN Q30066_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4grl" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC II 3D structures|MHC II 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 21: | Line 29: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sethi DK]] | ||
[[Category: | [[Category: Wucherpfennig KW]] | ||
Latest revision as of 13:02, 30 October 2024
Crystal structure of a autoimmune TCR-MHC complexCrystal structure of a autoimmune TCR-MHC complex
Structural highlights
FunctionPublication Abstract from PubMedSelf-reactive CD4 T cells are thought to have a central role in the pathogenesis of many chronic inflammatory human diseases. Microbial peptides can activate self-reactive T cells, but the structural basis for such crossreactivity is not well understood. The Hy.1B11 T cell receptor (TCR) originates from a patient with multiple sclerosis and recognizes the self-antigen myelin basic protein. Here we report the structural mechanism of TCR crossreactivity with two distinct peptides from human pathogens. The structures show that a single TCR residue (CDR3alpha F95) makes the majority of contacts with the self-peptide and both microbial peptides (66.7-80.6%) due to a highly tilted TCR-binding topology on the peptide-MHC surface. Further, a neighbouring residue located on the same TCR loop (CDR3alpha E98) forms an energetically critical interaction with the MHC molecule. These data show how binding by a self-reactive TCR favors crossreactivity between self and microbial antigens. Crossreactivity of a human autoimmune TCR is dominated by a single TCR loop.,Sethi DK, Gordo S, Schubert DA, Wucherpfennig KW Nat Commun. 2013 Oct 18;4:2623. doi: 10.1038/ncomms3623. PMID:24136005[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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