Regulating UBP-mediated ubiquitin deconjugation.
The first crystal structures have been obtained for a UBP domain both alone and in complex with ubiquitin aldehyde, thus providing a framework for structural conservation throughout the UBP protease family. Comparison of the structures provides substantial insight into ubiquitin-mediated activation of UBP protease activity, a process that potentially regulates substrate-dependent ubiquitin deconjugation.
Lima
Christopher D
CD
D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011485:Protein Binding; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7
D046911:Macromolecular Substances; D016159:Tumor Suppressor Protein p53; D025801:Ubiquitin; D010450:Endopeptidases; C464569:USP7 protein, human; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7; C059237:ubiquitin-Nalpha-protein hydrolase