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.
Enregistré dans:
Auteurs principaux: | Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, Ben E. Black, John M. Pascal |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2018
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/86fcef598c794822b2da2e8ca622e51d |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
A substrate-driven allosteric switch that enhances PDI catalytic activity
par: Roelof H. Bekendam, et autres
Publié: (2016) -
HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications
par: Marie-France Langelier, et autres
Publié: (2021) -
Mechanisms of Nucleosome Reorganization by PARP1
par: Natalya V. Maluchenko, et autres
Publié: (2021) -
Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
par: Zachary Maben, et autres
Publié: (2021) -
NAMPT-derived NAD+ fuels PARP1 to promote skin inflammation through parthanatos cell death.
par: Francisco J Martínez-Morcillo, et autres
Publié: (2021)