Alternative modes of client binding enable functional plasticity of Hsp70: letter

Hsp70 binds unfolded protein segments in its groove, but can also bind and stabilize folded protein structures, owing to its moveable lid, with ATP hydrolysis and co-chaperones allowing control of these contrasting effects.

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Bibliographic Details
Main Authors:	Mashaghi Tabari, Alireza (Author) , Bezrukavnikov, Sergey (Author) , Minde, David P. (Author) , Wentink, Anne (Author) , Kityk, Roman (Author) , Zachmann-Brand, Beate (Author) , Mayer, Matthias P. (Author) , Kramer, Günter (Author) , Bukau, Bernd (Author) , Tans, Sander J. (Author)
Format:	Article (Journal) Editorial
Language:	English
Published:	26 October 2016
In:	Nature Year: 2016, Volume: 539, Issue: 7629, Pages: 448-451
ISSN:	1476-4687
DOI:	10.1038/nature20137
Online Access:	Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nature20137 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nature20137
Author Notes:	Alireza Mashaghi, Sergey Bezrukavnikov, David P. Minde, Anne S. Wentink, Roman Kityk, Beate Zachmann-Brand, Matthias P. Mayer, Günter Kramer, Bernd Bukau & Sander J. Tans

Description
Summary:	Hsp70 binds unfolded protein segments in its groove, but can also bind and stabilize folded protein structures, owing to its moveable lid, with ATP hydrolysis and co-chaperones allowing control of these contrasting effects.
Item Description:	Gesehen am 12.05.2020
Physical Description:	Online Resource
ISSN:	1476-4687
DOI:	10.1038/nature20137