Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition

Poly(ADP-ribose) polymerase 2 (PARP2) is activated by 5′-phosphorylated DNA breaks but the molecular mechanism is not fully understood. Here, the authors report a crystal structure of PARP2 bound to an activating DNA fragment, providing insights into the structural changes that lead to PARP2 activat...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Ezeogo Obaji, Mirko M. Maksimainen, Albert Galera-Prat, Lari Lehtiö
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Q
Acceso en línea:https://doaj.org/article/3e12a12ec89744fea3a04b2b30548e8f
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:3e12a12ec89744fea3a04b2b30548e8f
record_format dspace
spelling oai:doaj.org-article:3e12a12ec89744fea3a04b2b30548e8f2021-12-02T14:59:27ZActivation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition10.1038/s41467-021-23800-x2041-1723https://doaj.org/article/3e12a12ec89744fea3a04b2b30548e8f2021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23800-xhttps://doaj.org/toc/2041-1723Poly(ADP-ribose) polymerase 2 (PARP2) is activated by 5′-phosphorylated DNA breaks but the molecular mechanism is not fully understood. Here, the authors report a crystal structure of PARP2 bound to an activating DNA fragment, providing insights into the structural changes that lead to PARP2 activation.Ezeogo ObajiMirko M. MaksimainenAlbert Galera-PratLari LehtiöNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Ezeogo Obaji
Mirko M. Maksimainen
Albert Galera-Prat
Lari Lehtiö
Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
description Poly(ADP-ribose) polymerase 2 (PARP2) is activated by 5′-phosphorylated DNA breaks but the molecular mechanism is not fully understood. Here, the authors report a crystal structure of PARP2 bound to an activating DNA fragment, providing insights into the structural changes that lead to PARP2 activation.
format article
author Ezeogo Obaji
Mirko M. Maksimainen
Albert Galera-Prat
Lari Lehtiö
author_facet Ezeogo Obaji
Mirko M. Maksimainen
Albert Galera-Prat
Lari Lehtiö
author_sort Ezeogo Obaji
title Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
title_short Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
title_full Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
title_fullStr Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
title_full_unstemmed Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
title_sort activation of parp2/artd2 by dna damage induces conformational changes relieving enzyme autoinhibition
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/3e12a12ec89744fea3a04b2b30548e8f
work_keys_str_mv AT ezeogoobaji activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
AT mirkommaksimainen activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
AT albertgaleraprat activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
AT larilehtio activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
_version_ 1718389194426941440