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==Crystal structure of a autoimmune TCR-MHC complex== | |||
=== | <StructureSection load='4grl' size='340' side='right' caption='[[4grl]], [[Resolution|resolution]] 2.86Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4grl]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GRL FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pl6|3pl6]], [[4may|4may]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alpha chain, HLA-DQ1, HLA-DQA1, MHC CLASS II MOLECULE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), beta chain, HLA-DQ1, HLA-DQB1, MHC CLASS II MOLECULE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), TCR Hy.1B11 alpha chain ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), TCR Hy.1B11 beta chain ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4grl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4grl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4grl RCSB], [http://www.ebi.ac.uk/pdbsum/4grl PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Self-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<ref>PMID:24136005</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Sethi, D K | [[Category: Sethi, D K]] | ||
[[Category: Wucherpfennig, K W | [[Category: Wucherpfennig, K W]] | ||
[[Category: Autoimmunity]] | [[Category: Autoimmunity]] | ||
[[Category: Immune complex]] | [[Category: Immune complex]] | ||
Revision as of 14:03, 21 December 2014
Crystal structure of a autoimmune TCR-MHC complexCrystal structure of a autoimmune TCR-MHC complex
Structural highlights
Publication 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. References
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