Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hs...

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Autores principales:	Javier Oroz, Bliss J. Chang, Piotr Wysoczanski, Chung-Tien Lee, Ángel Pérez-Lara, Pijush Chakraborty, Romina V. Hofele, Jeremy D. Baker, Laura J. Blair, Jacek Biernat, Henning Urlaub, Eckhard Mandelkow, Chad A. Dickey, Markus Zweckstetter
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3a370245b8a44bedbc69cc4763edff90
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spelling	oai:doaj.org-article:3a370245b8a44bedbc69cc4763edff902021-12-02T16:50:07ZStructure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex10.1038/s41467-018-06880-02041-1723https://doaj.org/article/3a370245b8a44bedbc69cc4763edff902018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06880-0https://doaj.org/toc/2041-1723The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hsp90/FKBP51 ternary complex using a NMR based integrative approach.Javier OrozBliss J. ChangPiotr WysoczanskiChung-Tien LeeÁngel Pérez-LaraPijush ChakrabortyRomina V. HofeleJeremy D. BakerLaura J. BlairJacek BiernatHenning UrlaubEckhard MandelkowChad A. DickeyMarkus ZweckstetterNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Javier Oroz Bliss J. Chang Piotr Wysoczanski Chung-Tien Lee Ángel Pérez-Lara Pijush Chakraborty Romina V. Hofele Jeremy D. Baker Laura J. Blair Jacek Biernat Henning Urlaub Eckhard Mandelkow Chad A. Dickey Markus Zweckstetter Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
description	The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hsp90/FKBP51 ternary complex using a NMR based integrative approach.
format	article
author	Javier Oroz Bliss J. Chang Piotr Wysoczanski Chung-Tien Lee Ángel Pérez-Lara Pijush Chakraborty Romina V. Hofele Jeremy D. Baker Laura J. Blair Jacek Biernat Henning Urlaub Eckhard Mandelkow Chad A. Dickey Markus Zweckstetter
author_facet	Javier Oroz Bliss J. Chang Piotr Wysoczanski Chung-Tien Lee Ángel Pérez-Lara Pijush Chakraborty Romina V. Hofele Jeremy D. Baker Laura J. Blair Jacek Biernat Henning Urlaub Eckhard Mandelkow Chad A. Dickey Markus Zweckstetter
author_sort	Javier Oroz
title	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_short	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_full	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_fullStr	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_full_unstemmed	Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex
title_sort	structure and pro-toxic mechanism of the human hsp90/ppiase/tau complex
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/3a370245b8a44bedbc69cc4763edff90
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Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

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