Ontology highlight
ABSTRACT:
SUBMITTER: Kim RQ
PROVIDER: S-EPMC6335408 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
Kim Robbert Q RQ Geurink Paul P PP Mulder Monique P C MPC Fish Alexander A Ekkebus Reggy R El Oualid Farid F van Dijk Willem J WJ van Dalen Duco D Ovaa Huib H van Ingen Hugo H Sixma Titia K TK
Nature communications 20190116 1
USP7 is a highly abundant deubiquitinating enzyme (DUB), involved in cellular processes including DNA damage response and apoptosis. USP7 has an unusual catalytic mechanism, where the low intrinsic activity of the catalytic domain (CD) increases when the C-terminal Ubl domains (Ubl45) fold onto the CD, allowing binding of the activating C-terminal tail near the catalytic site. Here we delineate how the target protein promotes the activation of USP7. Using NMR analysis and biochemistry we describ ...[more]