| Literature DB >> 15567417 |
David Reverter1, Kenneth Wu, Tudeviin Gan Erdene, Zhen-Qiang Pan, Keith D Wilkinson, Christopher D Lima.
Abstract
The Nedd8 conjugation pathway is conserved from yeast to humans and is essential in many organisms. Nedd8 is conjugated to cullin proteins in a process that alters SCF E3 ubiquitin ligase activity, and it is presumed that Nedd8 deconjugation would reverse these effects. We now report the X-ray structures of the human Nedd8-specific protease, Den1, in a complex with the inhibitor Nedd8 aldehyde, thus revealing a model for the tetrahedral transition state intermediate generated during proteolysis. Although Den1 is closely related to the SUMO-specific protease family (Ulp/Senp family), structural analysis of the interface suggests determinants involved in Nedd8 selectivity by Den1 over other ubiquitin-like family members and suggests how the Ulp/Senp architecture has been modified to interact with different ubiquitin-like modifiers.Entities:
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Year: 2005 PMID： 15567417 DOI： 10.1016/j.jmb.2004.10.022
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469