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• W2024431726 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." @default.
• W2024431726 created "2016-06-24" @default.
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• W2024431726 date "2005-01-01" @default.
• W2024431726 modified "2023-10-10" @default.
• W2024431726 title "Structure of a Complex between Nedd8 and the Ulp/Senp Protease Family Member Den1" @default.
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• W2024431726 doi "https://doi.org/10.1016/j.jmb.2004.10.022" @default.
• W2024431726 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15567417" @default.
• W2024431726 hasPublicationYear "2005" @default.
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