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8f2r: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8f2r]] is a 10 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=8F2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F2R FirstGlance]. <br>
<table><tr><td colspan='2'>[[8f2r]] is a 10 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=8F2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F2R FirstGlance]. <br>
</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=8f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f2r OCA], [https://pdbe.org/8f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f2r RCSB], [https://www.ebi.ac.uk/pdbsum/8f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f2r ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.12&#8491;</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=8f2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f2r OCA], [https://pdbe.org/8f2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f2r RCSB], [https://www.ebi.ac.uk/pdbsum/8f2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f2r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/COMD1_HUMAN COMD1_HUMAN] Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.<ref>PMID:14685266</ref> <ref>PMID:15799966</ref> <ref>PMID:16573520</ref> <ref>PMID:17309234</ref> <ref>PMID:17183367</ref> <ref>PMID:20048074</ref> <ref>PMID:20595380</ref>  
[https://www.uniprot.org/uniprot/COMD1_HUMAN COMD1_HUMAN] Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.<ref>PMID:14685266</ref> <ref>PMID:15799966</ref> <ref>PMID:16573520</ref> <ref>PMID:17309234</ref> <ref>PMID:17183367</ref> <ref>PMID:20048074</ref> <ref>PMID:20595380</ref>  
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== Publication Abstract from PubMed ==
The Commander complex is required for endosomal recycling of diverse transmembrane cargos and is mutated in Ritscher-Schinzel syndrome. It comprises two sub-assemblies: Retriever composed of VPS35L, VPS26C, and VPS29; and the CCC complex which contains twelve subunits: COMMD1-COMMD10 and the coiled-coil domain-containing (CCDC) proteins CCDC22 and CCDC93. Combining X-ray crystallography, electron cryomicroscopy, and in silico predictions, we have assembled a complete structural model of Commander. Retriever is distantly related to the endosomal Retromer complex but has unique features preventing the shared VPS29 subunit from interacting with Retromer-associated factors. The COMMD proteins form a distinctive hetero-decameric ring stabilized by extensive interactions with CCDC22 and CCDC93. These adopt a coiled-coil structure that connects the CCC and Retriever assemblies and recruits a 16th subunit, DENND10, to form the complete Commander complex. The structure allows mapping of disease-causing mutations and reveals the molecular features required for the function of this evolutionarily conserved trafficking machinery.
Structure of the endosomal Commander complex linked to Ritscher-Schinzel syndrome.,Healy MD, McNally KE, Butkovic R, Chilton M, Kato K, Sacharz J, McConville C, Moody ERR, Shaw S, Planelles-Herrero VJ, Yadav SKN, Ross J, Borucu U, Palmer CS, Chen KE, Croll TI, Hall RJ, Caruana NJ, Ghai R, Nguyen THD, Heesom KJ, Saitoh S, Berger I, Schaffitzel C, Williams TA, Stroud DA, Derivery E, Collins BM, Cullen PJ Cell. 2023 May 11;186(10):2219-2237.e29. doi: 10.1016/j.cell.2023.04.003. PMID:37172566<ref>PMID:37172566</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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