3pl6: Difference between revisions
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==Structure of Autoimmune TCR Hy.1B11 in complex with HLA-DQ1 and MBP 85-99== | ==Structure of Autoimmune TCR Hy.1B11 in complex with HLA-DQ1 and MBP 85-99== | ||
<StructureSection load='3pl6' size='340' side='right' caption='[[3pl6]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='3pl6' size='340' side='right'caption='[[3pl6]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pl6]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3pl6]] 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=3PL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PL6 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]] 2.55Å</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=3pl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pl6 OCA], [https://pdbe.org/3pl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pl6 RCSB], [https://www.ebi.ac.uk/pdbsum/3pl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pl6 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/A0A173ADG5_HUMAN A0A173ADG5_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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 3pl6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[T-cell receptor|T-cell receptor]] | *[[MHC 3D structures|MHC 3D structures]] | ||
*[[MHC II 3D structures|MHC II 3D structures]] | |||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sethi DK]] | ||
[[Category: | [[Category: Wucherpfennig KW]] | ||
Latest revision as of 12:33, 30 October 2024
Structure of Autoimmune TCR Hy.1B11 in complex with HLA-DQ1 and MBP 85-99Structure of Autoimmune TCR Hy.1B11 in complex with HLA-DQ1 and MBP 85-99
Structural highlights
FunctionPublication Abstract from PubMedSelf-reactive T cells that escape elimination in the thymus can cause autoimmune pathology, and it is therefore important to understand the structural mechanisms of self-antigen recognition. We report the crystal structure of a T cell receptor (TCR) from a patient with relapsing-remitting multiple sclerosis that engages its self-peptide-major histocompatibility complex (pMHC) ligand in an unusual manner. The TCR is bound in a highly tilted orientation that prevents interaction of the TCR-alpha chain with the MHC class II beta chain helix. In this structure, only a single germline-encoded TCR loop engages the MHC protein, whereas in most other TCR-pMHC structures all four germline-encoded TCR loops bind to the MHC helices. The tilted binding mode also prevents peptide contacts by the short complementarity-determining region (CDR) 3beta loop, and interactions that contribute to peptide side chain specificity are focused on the CDR3alpha loop. This structure is the first example in which only a single germline-encoded TCR loop contacts the MHC helices. Furthermore, the reduced interaction surface with the peptide may facilitate TCR cross-reactivity. The structural alterations in the trimolecular complex are distinct from previously characterized self-reactive TCRs, indicating that there are multiple unusual ways for self-reactive TCRs to bind their pMHC ligand. A highly tilted binding mode by a self-reactive T cell receptor results in altered engagement of peptide and MHC.,Sethi DK, Schubert DA, Anders AK, Heroux A, Bonsor DA, Thomas CP, Sundberg EJ, Pyrdol J, Wucherpfennig KW J Exp Med. 2011 Jan 17;208(1):91-102. Epub 2011 Jan 3. PMID:21199956[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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