|
|
| Line 3: |
Line 3: |
| <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 [https://en.wikipedia.org/wiki/Human Human]. 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> | | <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='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> | | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ymm|1ymm]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-DQA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HLA-DQB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=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'>[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> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A0A0A8WFP6_HUMAN A0A0A8WFP6_HUMAN] |
| Self-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<ref>PMID:21199956</ref>
| |
| | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 3pl6" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| | *[[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/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Sethi, D K]] | | [[Category: Sethi DK]] |
| [[Category: Wucherpfennig, K W]] | | [[Category: Wucherpfennig KW]] |
| [[Category: Immune receptor]]
| |
| [[Category: Immune system]]
| |
| [[Category: Immunoglobulin fold]]
| |
| [[Category: Membrane]]
| |
| [[Category: Tcr-mhc complex]]
| |