4a3o: Difference between revisions

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-==CRYSTAL STRUCTURE OF THE USP15 DUSP-UBL MONOMER==
-<StructureSection load='4a3o' size='340' side='right' caption='[[4a3o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+==Crystal structure of the USP15 DUSP-UBL monomer==
+<StructureSection load='4a3o' size='340' side='right'caption='[[4a3o]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4a3o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A3O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4a3o]] is a 2 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=4A3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3O FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><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]] 2.2&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w6v|1w6v]], [[4a3p|4a3p]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></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=4a3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3o OCA], [https://pdbe.org/4a3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3o RCSB], [https://www.ebi.ac.uk/pdbsum/4a3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3o ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a3o RCSB], [http://www.ebi.ac.uk/pdbsum/4a3o PDBsum]</span></td></tr>
+</table>
-<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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4a3o" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Thioesterase|Thioesterase]]
+*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 == References ==
 <references/>
@@ Line 24: / Line 27: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Ubiquitinyl hydrolase 1]]
+[[Category: Large Structures]]
-[[Category: Barsukov, I L.]]
+[[Category: Barsukov IL]]
-[[Category: Clague, M J.]]
+[[Category: Clague MJ]]
-[[Category: Elliott, P R.]]
+[[Category: Elliott PR]]
-[[Category: Grossmann, G J.]]
+[[Category: Grossmann GJ]]
-[[Category: Liu, H.]]
+[[Category: Liu H]]
-[[Category: Pastok, M W.]]
+[[Category: Pastok MW]]
-[[Category: Rigden, D J.]]
+[[Category: Rigden DJ]]
-[[Category: Urbe, S.]]
+[[Category: Urbe S]]
-[[Category: Hydrolase]]