Ontology highlight
ABSTRACT:
SUBMITTER: Wang Z
PROVIDER: S-EPMC3897571 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Wang Zhizhi Z Gagné Jean-Philippe JP Poirier Guy G GG Xu Wenqing W
PloS one 20140121 1
Protein poly(ADP-ribosyl)ation (PARylation) regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase (PARG) is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) (PAR) polymer in vivo. Here we report crystal structures of the mouse PARG (mPARG) catalytic domain, its complexes with ADP-ribose (ADPr) and a PARG inhibitor ADP-HPD, as well as four PARG catalytic residues mutants. With these structures and biochemical analysis of 20 mPARG mutants, we provid ...[more]