6cpm
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of the USP15 deubiquitinase domain in complex with a third-generation inhibitory Ubv== | |
+ | <StructureSection load='6cpm' size='340' side='right'caption='[[6cpm]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6cpm]] 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=6CPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CPM FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.011Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6cpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpm OCA], [https://pdbe.org/6cpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cpm RCSB], [https://www.ebi.ac.uk/pdbsum/6cpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpm ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref> | ||
- | + | ==See Also== | |
- | + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] | |
- | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: Lenter | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Boehmelt G]] |
+ | [[Category: Lenter M]] | ||
+ | [[Category: Sicheri F]] | ||
+ | [[Category: Sidhu SS]] | ||
+ | [[Category: Singer AU]] | ||
+ | [[Category: Teyra J]] |
Current revision
Structure of the USP15 deubiquitinase domain in complex with a third-generation inhibitory Ubv
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Categories: Homo sapiens | Large Structures | Boehmelt G | Lenter M | Sicheri F | Sidhu SS | Singer AU | Teyra J