2y6e | pdb_00002y6e

Ubiquitin Specific Protease 4 is inhibited by its Ubiquitin-like domain

spinqualitylabelsall models 2y6e, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y6e is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4, ZN NonStd Res: CME Activity: Ubiquitin thiolesterase, with EC number 3.1.2.15 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed USP4 is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes that has a role in spliceosome regulation. Here, we show that the crystal structure of the minimal catalytic domain of USP4 has the conserved USP-like fold with its typical ubiquitin-binding site. A ubiquitin-like (Ubl) domain inserted into the catalytic domain has autoregulatory function. This Ubl domain can bind to the catalytic domain and compete with the ubiquitin substrate, partially inhibiting USP4 activity against different substrates. Interestingly, other USPs, such as USP39, could relieve this inhibition. Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain.,Luna-Vargas MP, Faesen AC, van Dijk WJ, Rape M, Fish A, Sixma TK EMBO Rep. 2011 Apr 1;12(4):365-72. Epub 2011 Mar 18. PMID:21415856 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioesterase

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