Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site-Reference-Cited by-同舟云学术

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Structural and Functional Analysis of GRP94 in the Closed State Reveals an Essential Role for the Pre-N Domain and a Potential Client-Binding Site

Published:2017-09 Issue:12 Volume:20 Page:2800-2809
ISSN:2211-1247
Container-title:Cell Reports
language:en
Short-container-title:Cell Reports

Author:

Huck John D.,Que Nanette L.,Hong Feng,Li Zihai,Gewirth Daniel T.

Funder

NIH

Richard and Mae Stone Goode Foundation of Buffalo

Avon Foundation

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference43 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution;Adams;Acta Crystallogr. D Biol. Crystallogr.,2010

2. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex;Ali;Nature,2006

3. Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94;Ansa-Addo;Curr. Top. Med. Chem.,2016

4. A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein 90 is required for resistance to tunicamycin or high calcium-induced ER stresses;Chong;J. Exp. Bot.,2015

5. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones;Dollins;Mol. Cell,2007

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