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

Marie-France Langelier; Levani Zandarashvili; Pedro M. Aguiar; Ben E. Black; John M. Pascal

doi:10.1038/s41467-018-03234-8

Nature Communications (Feb 2018)

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

Marie-France Langelier,
Levani Zandarashvili,
Pedro M. Aguiar,
Ben E. Black,
John M. Pascal

Affiliations

Marie-France Langelier: Department of Biochemistry and Molecular Medicine, Université de Montréal
Levani Zandarashvili: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania
Pedro M. Aguiar: Department of Chemistry, Université de Montréal
Ben E. Black: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania
John M. Pascal: Department of Biochemistry and Molecular Medicine, Université de Montréal

DOI: https://doi.org/10.1038/s41467-018-03234-8
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 13

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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