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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Autores principales:	Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, Ben E. Black, John M. Pascal
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/86fcef598c794822b2da2e8ca622e51d
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spelling	oai:doaj.org-article:86fcef598c794822b2da2e8ca622e51d2021-12-02T15:34:06ZNAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains10.1038/s41467-018-03234-82041-1723https://doaj.org/article/86fcef598c794822b2da2e8ca622e51d2018-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03234-8https://doaj.org/toc/2041-1723Poly(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.Marie-France LangelierLevani ZandarashviliPedro M. AguiarBen E. BlackJohn M. PascalNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Marie-France Langelier Levani Zandarashvili Pedro M. Aguiar Ben E. Black John M. Pascal NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
description	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.
format	article
author	Marie-France Langelier Levani Zandarashvili Pedro M. Aguiar Ben E. Black John M. Pascal
author_facet	Marie-France Langelier Levani Zandarashvili Pedro M. Aguiar Ben E. Black John M. Pascal
author_sort	Marie-France Langelier
title	NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
title_short	NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
title_full	NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
title_fullStr	NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
title_full_unstemmed	NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains
title_sort	nad+ analog reveals parp-1 substrate-blocking mechanism and allosteric communication from catalytic center to dna-binding domains
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/86fcef598c794822b2da2e8ca622e51d
work_keys_str_mv	AT mariefrancelangelier nadanalogrevealsparp1substrateblockingmechanismandallostericcommunicationfromcatalyticcentertodnabindingdomains AT levanizandarashvili nadanalogrevealsparp1substrateblockingmechanismandallostericcommunicationfromcatalyticcentertodnabindingdomains AT pedromaguiar nadanalogrevealsparp1substrateblockingmechanismandallostericcommunicationfromcatalyticcentertodnabindingdomains AT beneblack nadanalogrevealsparp1substrateblockingmechanismandallostericcommunicationfromcatalyticcentertodnabindingdomains AT johnmpascal nadanalogrevealsparp1substrateblockingmechanismandallostericcommunicationfromcatalyticcentertodnabindingdomains
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NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains

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