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6yxe
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Trim69 RING domain== | |
| + | <StructureSection load='6yxe' size='340' side='right'caption='[[6yxe]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6yxe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YXE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6YXE FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRIM69, RNF36, HSD-34, HSD34 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6yxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yxe OCA], [http://pdbe.org/6yxe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6yxe RCSB], [http://www.ebi.ac.uk/pdbsum/6yxe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6yxe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TRI69_HUMAN TRI69_HUMAN]] May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis.<ref>PMID:23131556</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Members of the TRIM protein family have been shown to inhibit a range of viral infections. Recently, TRIM69 was identified as a potent inhibitor of Vesicular stomatitis Indiana virus infection, with its inhibition being dependent upon multimerization. Using SEC-MALLS analysis, it is demonstrated that the assembly of TRIM69 is mediated through the RING domain and not the Bbox domain as has been shown for other TRIM proteins. Using X-ray crystallography, the structure of the TRIM69 RING domain has been determined to a resolution of 2.1 A, the oligomerization interface has been identified and regions outside the four-helix bundle have been observed to form interactions that are likely to support assembly. | ||
| - | + | The RING domain of TRIM69 promotes higher-order assembly.,Keown JR, Yang J, Black MM, Goldstone DC Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):954-961. doi:, 10.1107/S2059798320010499. Epub 2020 Sep 16. PMID:33021497<ref>PMID:33021497</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6yxe" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: RING-type E3 ubiquitin transferase]] | ||
| + | [[Category: Goldstone, D C]] | ||
| + | [[Category: Keown, J R]] | ||
| + | [[Category: Antiviral protein]] | ||
| + | [[Category: Trim protein]] | ||
| + | [[Category: Trim69]] | ||
| + | [[Category: Tripartite motif]] | ||
Current revision
Structure of the Trim69 RING domain
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