NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains

Poly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the mechanism of PARP-1 allosteric regulation.

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Auteurs principaux: Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, Ben E. Black, John M. Pascal
Format: article
Langue:EN
Publié: Nature Portfolio 2018
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Accès en ligne:https://doaj.org/article/86fcef598c794822b2da2e8ca622e51d
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Résumé:Poly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the mechanism of PARP-1 allosteric regulation.