View source for 8p0x


==Structure of the human Commander complex Retriever Subcomplex==
<StructureSection load='8p0x' size='340' side='right'caption='[[8p0x]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8p0x]] is a 5 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=8P0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P0X FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5&#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=8p0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p0x OCA], [https://pdbe.org/8p0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p0x RCSB], [https://www.ebi.ac.uk/pdbsum/8p0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p0x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCD93_HUMAN CCD93_HUMAN] Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1 (PubMed:25355947, PubMed:28892079). Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with WASHC2C (PubMed:25355947).<ref>PMID:25355947</ref> <ref>PMID:28892079</ref>   (Microbial infection) The CCC complex, in collaboration with the heterotrimeric retriever complex, mediates the exit of human papillomavirus to the cell surface.<ref>PMID:28892079</ref> 
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== Publication Abstract from PubMed ==
The Commander complex, a 16-protein assembly, plays multiple roles in cell homeostasis, cell cycle and immune response. It consists of copper-metabolism Murr1 domain proteins (COMMD1-10), coiled-coil domain-containing proteins (CCDC22 and CCDC93), DENND10 and the Retriever subcomplex (VPS26C, VPS29 and VPS35L), all expressed ubiquitously in the body and linked to various diseases. Here, we report the structure and key interactions of the endogenous human Commander complex by cryogenic-electron microscopy and mass spectrometry-based proteomics. The complex consists of a stable core of COMMD1-10 and an effector containing DENND10 and Retriever, scaffolded together by CCDC22 and CCDC93. We establish the composition of Commander and reveal major interaction interfaces. These findings clarify its roles in intracellular transport, and uncover a strong association with cilium assembly, and centrosome and centriole functions.

Structure and interactions of the endogenous human Commander complex.,Laulumaa S, Kumpula EP, Huiskonen JT, Varjosalo M Nat Struct Mol Biol. 2024 Jun;31(6):925-938. doi: 10.1038/s41594-024-01246-1. , Epub 2024 Mar 8. PMID:38459129<ref>PMID:38459129</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8p0x" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Huiskonen JT]]
[[Category: Kumpula EP]]
[[Category: Laulumaa S]]