4z8m

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(New page: '''Unreleased structure''' The entry 4z8m is ON HOLD Authors: Shi, Z., Zhou, Z. Description: Crystal structure of MT complex Category: Unreleased Structures Category: Zhou, Z [...)
Current revision (15:42, 8 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4z8m is ON HOLD
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==Crystal structure of the MAVS-TRAF6 complex==
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<StructureSection load='4z8m' size='340' side='right'caption='[[4z8m]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4z8m]] 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=4Z8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z8M FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4z8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z8m OCA], [https://pdbe.org/4z8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z8m RCSB], [https://www.ebi.ac.uk/pdbsum/4z8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z8m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRAF6_HUMAN TRAF6_HUMAN] E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN. May be essential for the formation of functional osteoclasts. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation.<ref>PMID:8837778</ref> <ref>PMID:11057907</ref> <ref>PMID:16378096</ref> <ref>PMID:17135271</ref> <ref>PMID:18093978</ref> <ref>PMID:18758450</ref> <ref>PMID:19675569</ref> <ref>PMID:19713527</ref> <ref>PMID:12140561</ref> <ref>PMID:19465916</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In response to viral infection, cytosolic retinoic acid-inducible gene I-like receptors sense viral RNA and promote oligomerization of mitochondrial antiviral signaling protein (MAVS), which then recruits tumor necrosis factor receptor-associated factor (TRAF) family proteins, including TRAF6, to activate an antiviral response. Currently, the interaction between MAVS and TRAF6 is only partially understood, and atomic details are lacking. Here, we demonstrated that MAVS directly interacts with TRAF6 through its potential TRAF6-binding motif 2 (T6BM2; amino acids 455-460). Further, we solved the crystal structure of MAVS T6BM2 in complex with the TRAF6 TRAF_C domain at 2.95 A resolution. T6BM2 of MAVS binds to the canonical adaptor-binding groove of the TRAF_C domain. Structure-directed mutational analyses in vitro and in cells revealed that MAVS binding to TRAF6 via T6BM2 instead of T6BM1 is essential but not sufficient for an optimal antiviral response. Particularly, a MAVS mutant Y460E retained its TRAF6-binding ability as predicted but showed significantly impaired signaling activity, highlighting the functional importance of this tyrosine. Moreover, these observations were further confirmed in MAVS(-/-) mouse embryonic fibroblast cells. Collectively, our work provides a structural basis for understanding the MAVS-TRAF6 antiviral response.
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Authors: Shi, Z., Zhou, Z.
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Structural Insights into Mitochondrial Antiviral Signaling Protein (MAVS)-Tumor Necrosis Factor Receptor-associated Factor 6 (TRAF6) Signaling.,Shi Z, Zhang Z, Zhang Z, Wang Y, Li C, Wang X, He F, Sun L, Jiao S, Shi W, Zhou Z J Biol Chem. 2015 Oct 30;290(44):26811-20. doi: 10.1074/jbc.M115.666578. Epub, 2015 Sep 18. PMID:26385923<ref>PMID:26385923</ref>
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Description: Crystal structure of MT complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zhou, Z]]
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<div class="pdbe-citations 4z8m" style="background-color:#fffaf0;"></div>
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[[Category: Shi, Z]]
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==See Also==
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*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Shi ZB]]
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[[Category: Zhou Z]]

Current revision

Crystal structure of the MAVS-TRAF6 complex

PDB ID 4z8m

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