Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase
作者： Mark S. Dunstan , Eva Barkauskaite , Pierre Lafite , Claire E. Knezevic , Amy Brassington
DOI: 10.1038/NCOMMS1889
关键词:
摘要: Poly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of number cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion poly(ADP-ribosyl)ation catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets unique PAR (1''-2') ribose-ribose bonds. Here we report structure mechanism first canonical PARG from protozoan Tetrahymena thermophila. In addition, reveal T. thermophila complex with novel rhodanine-containing mammalian inhibitor RBPI-3. Our data demonstrate that represents good model for human therefore likely to prove useful guiding structure-based discovery new classes inhibitors.
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