Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative

The human AAA+protein p97 plays an important role in cellular protein homeostasis. Here, the authors use cryo-EM to obtain further insights into how p97 interacts with its co-factor Npl4 and they observe three distinct conformational states of Npl4 in complex with human p97, which suggests that a se...

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Autores principales:	Man Pan, Qingyun Zheng, Yuanyuan Yu, Huasong Ai, Yuan Xie, Xin Zeng, Chu Wang, Lei Liu, Minglei Zhao
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/d5a2805ae530457a97408aaa4fbfe72d
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spelling	oai:doaj.org-article:d5a2805ae530457a97408aaa4fbfe72d2021-12-02T15:16:22ZSeesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative10.1038/s41467-020-20359-x2041-1723https://doaj.org/article/d5a2805ae530457a97408aaa4fbfe72d2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20359-xhttps://doaj.org/toc/2041-1723The human AAA+protein p97 plays an important role in cellular protein homeostasis. Here, the authors use cryo-EM to obtain further insights into how p97 interacts with its co-factor Npl4 and they observe three distinct conformational states of Npl4 in complex with human p97, which suggests that a seesaw motion is essential for the unfolding activity of the p97 complex.Man PanQingyun ZhengYuanyuan YuHuasong AiYuan XieXin ZengChu WangLei LiuMinglei ZhaoNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Man Pan Qingyun Zheng Yuanyuan Yu Huasong Ai Yuan Xie Xin Zeng Chu Wang Lei Liu Minglei Zhao Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
description	The human AAA+protein p97 plays an important role in cellular protein homeostasis. Here, the authors use cryo-EM to obtain further insights into how p97 interacts with its co-factor Npl4 and they observe three distinct conformational states of Npl4 in complex with human p97, which suggests that a seesaw motion is essential for the unfolding activity of the p97 complex.
format	article
author	Man Pan Qingyun Zheng Yuanyuan Yu Huasong Ai Yuan Xie Xin Zeng Chu Wang Lei Liu Minglei Zhao
author_facet	Man Pan Qingyun Zheng Yuanyuan Yu Huasong Ai Yuan Xie Xin Zeng Chu Wang Lei Liu Minglei Zhao
author_sort	Man Pan
title	Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
title_short	Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
title_full	Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
title_fullStr	Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
title_full_unstemmed	Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
title_sort	seesaw conformations of npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/d5a2805ae530457a97408aaa4fbfe72d
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Seesaw conformations of Npl4 in the human p97 complex and the inhibitory mechanism of a disulfiram derivative

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