Abstract
Molecular mechanism for the substrate recognition of USP7.
Highlights
The ubiquitin specific protease 7 (USP7), known as herpes virus associated ubiquitin specific protease (HAUSP), is a well-characterized deubiquitinase (ReyesTurcu et al, 2009)
Our previous study indicates that the KG-Linker of DNMT1 binds to TUDUSP7 and plays an important role in mediating DNMT1-USP7 interaction and USP7-mediated stabilization of DNMT1
DNMT1 and USP7-ICP0 indicates that ICP0 and KG-LinkerDNMT1 pack against the same acidic pocket of TUDUSP7 in an opposite orientation (Cheng et al, 2015)
Summary
The ubiquitin specific protease 7 (USP7), known as herpes virus associated ubiquitin specific protease (HAUSP), is a well-characterized deubiquitinase (ReyesTurcu et al, 2009). It has been shown that ICP0 peptide (residues 594–633) interacts with the TUD of USP7 (Everett et al, 1999). As indicated in the TUDUSP7-ICP0 structure, the interaction is mediated by a network of hydrogen bonds and salt bridge contacts.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
