Ontology highlight
ABSTRACT:
SUBMITTER: Phillips AH
PROVIDER: S-EPMC3710810 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20130625 28
Ubiquitin is a highly conserved eukaryotic protein that interacts with a diverse set of partners to act as a cellular signaling hub. Ubiquitin's conformational flexibility has been postulated to underlie its multifaceted recognition. Here we use computational and library-based means to interrogate core mutations that modulate the conformational dynamics of human ubiquitin. These ubiquitin variants exhibit increased affinity for the USP14 deubiquitinase, with concomitantly reduced affinity for ot ...[more]