4may: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4may]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Herpesviridae_sp. Herpesviridae sp.] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MAY FirstGlance]. <br> | <table><tr><td colspan='2'>[[4may]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Herpesviridae_sp. Herpesviridae sp.] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MAY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4may FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4may OCA], [https://pdbe.org/4may PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4may RCSB], [https://www.ebi.ac.uk/pdbsum/4may PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4may 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=4may FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4may OCA], [https://pdbe.org/4may PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4may RCSB], [https://www.ebi.ac.uk/pdbsum/4may PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4may ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 06:14, 21 November 2024
Crystal structure of an immune complexCrystal structure of an immune 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. References
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