Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Luna-Vargas MP, Faesen AC, van Dijk WJ, Rape M, Fish A, Sixma TK. Ubiquitin-specific protease 4 is inhibited by its ubiquitin-like domain. EMBO Rep. 2011 Apr 1;12(4):365-72. Epub 2011 Mar 18. PMID:21415856 doi:10.1038/embor.2011.33
