Alternative modes of client binding enable functional plasticity of Hsp70

Alireza Mashaghi, Sergey Bezrukavnikov, David P. Minde, Anne S. Wentink, Roman Kityk, Beate Zachmann-Brand, Matthias P. Mayer, Günter Kramer, Bernd Bukau and Sander J. Tans ()
Additional contact information
Alireza Mashaghi: FOM institute AMOLF
Sergey Bezrukavnikov: FOM institute AMOLF
David P. Minde: FOM institute AMOLF
Anne S. Wentink: Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
Roman Kityk: Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
Beate Zachmann-Brand: Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
Matthias P. Mayer: Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
Günter Kramer: Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
Bernd Bukau: Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance
Sander J. Tans: FOM institute AMOLF

Nature, 2016, vol. 539, issue 7629, 448-451

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature20137

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