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

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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Main Authors: 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
Format: article
Language:EN
Published: Nature Portfolio 2018
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Science
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Online Access:https://doaj.org/article/3a370245b8a44bedbc69cc4763edff90
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Summary: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.

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