Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

被引：0
|
作者：
Zhuo Li
F Ulrich Hartl
Andreas Bracher
机构：
[1] Max Planck Institute of Biochemistry,Department of Cellular Biochemistry
[2] Munich Center for Integrated Protein Science,Department of Chemistry and Biochemistry
来源：
Nature Structural & Molecular Biology | 2013年 / 20卷
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摘要：
The protein Hip interacts with chaperone Hsp70 and slows ADP dissociation from Hsp70, thus resulting in a delay in substrate release. Now crystal structures of Hip domains alone or in complex with Hsp70 nucleotide-binding domain, along with biochemical analyses, explain how Hip performs its activities.
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页码：929 / 935
页数：6
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