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

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...

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Main Authors: Ezeogo Obaji, Mirko M. Maksimainen, Albert Galera-Prat, Lari Lehtiö
Format: Article
Language:English
Published: Nature Publishing Group 2021-06-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23800-x
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spelling doaj-3e12a12ec89744fea3a04b2b30548e8f2021-06-13T11:15:57ZengNature Publishing GroupNature Communications2041-17232021-06-011211810.1038/s41467-021-23800-xActivation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibitionEzeogo Obaji0Mirko M. Maksimainen1Albert Galera-Prat2Lari Lehtiö3Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of OuluFaculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of OuluFaculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of OuluFaculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of OuluPoly(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.https://doi.org/10.1038/s41467-021-23800-x
collection DOAJ
language English
format Article
sources DOAJ
author Ezeogo Obaji
Mirko M. Maksimainen
Albert Galera-Prat
Lari Lehtiö
spellingShingle Ezeogo Obaji
Mirko M. Maksimainen
Albert Galera-Prat
Lari Lehtiö
Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-06-01
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.
url https://doi.org/10.1038/s41467-021-23800-x
work_keys_str_mv AT ezeogoobaji activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
AT mirkommaksimainen activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
AT albertgaleraprat activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
AT larilehtio activationofparp2artd2bydnadamageinducesconformationalchangesrelievingenzymeautoinhibition
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