Crystallographic and Biochemical Analysis of the Mouse Poly(ADP-Ribose) Glycohydrolase
作者： Zhizhi Wang , Jean-Philippe Gagné , Guy G. Poirier , Wenqing Xu
DOI: 10.1371/JOURNAL.PONE.0086010
关键词:
摘要: 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 poly(ADP-ribose) (PAR) polymer in vivo. Here we report crystal structures mouse PARG (mPARG) catalytic domain, its complexes with ADP-ribose (ADPr) and inhibitor ADP-HPD, as well four residues mutants. With these biochemical analysis 20 mPARG mutants, provide structural basis understanding how PAR recognized hydrolyzed by mPARG. The activity complementation experiment also suggest N-terminal flexible peptide preceding domain may regulate enzymatic PARG. This study contributes to our regulatory mechanisms rational design inhibitors.
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