Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s

Hsp70s are highly conserved molecular chaperones that play multiple essential roles in maintaining cellular protein homeostasis. Here, the authors provide structural evidence for active substrate release by Hsp70s upon ATP binding and provide insight into the molecular mechanism of ATP-driven Hsp70...

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Autores principales:	Jiao Yang, Yinong Zong, Jiayue Su, Hongtao Li, Huanyu Zhu, Linda Columbus, Lei Zhou, Qinglian Liu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/96c59e172310474e9274be9a59826a04
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spelling	oai:doaj.org-article:96c59e172310474e9274be9a59826a042021-12-02T14:40:37ZConformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s10.1038/s41467-017-01310-z2041-1723https://doaj.org/article/96c59e172310474e9274be9a59826a042017-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01310-zhttps://doaj.org/toc/2041-1723Hsp70s are highly conserved molecular chaperones that play multiple essential roles in maintaining cellular protein homeostasis. Here, the authors provide structural evidence for active substrate release by Hsp70s upon ATP binding and provide insight into the molecular mechanism of ATP-driven Hsp70 chaperone activity.Jiao YangYinong ZongJiayue SuHongtao LiHuanyu ZhuLinda ColumbusLei ZhouQinglian LiuNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jiao Yang Yinong Zong Jiayue Su Hongtao Li Huanyu Zhu Linda Columbus Lei Zhou Qinglian Liu Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s
description	Hsp70s are highly conserved molecular chaperones that play multiple essential roles in maintaining cellular protein homeostasis. Here, the authors provide structural evidence for active substrate release by Hsp70s upon ATP binding and provide insight into the molecular mechanism of ATP-driven Hsp70 chaperone activity.
format	article
author	Jiao Yang Yinong Zong Jiayue Su Hongtao Li Huanyu Zhu Linda Columbus Lei Zhou Qinglian Liu
author_facet	Jiao Yang Yinong Zong Jiayue Su Hongtao Li Huanyu Zhu Linda Columbus Lei Zhou Qinglian Liu
author_sort	Jiao Yang
title	Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s
title_short	Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s
title_full	Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s
title_fullStr	Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s
title_full_unstemmed	Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s
title_sort	conformation transitions of the polypeptide-binding pocket support an active substrate release from hsp70s
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/96c59e172310474e9274be9a59826a04
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Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s

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