The C-Terminal BAG Domain of BAG5 Induces Conformational Changes of the Hsp70 Nucleotide- Binding Domain for ADP-ATP Exchange-Reference-Cited by-同舟云学术

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The C-Terminal BAG Domain of BAG5 Induces Conformational Changes of the Hsp70 Nucleotide- Binding Domain for ADP-ATP Exchange

Published:2010-03 Issue:3 Volume:18 Page:309-319
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Arakawa Akihiko,Handa Noriko,Ohsawa Noboru,Shida Meiri,Kigawa Takanori,Hayashi Fumiaki,Shirouzu Mikako,Yokoyama Shigeyuki

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference53 articles.

1. Hsp110 is a nucleotide-activated exchange factor for Hsp70;Andreasson;J. Biol. Chem.,2008

2. Allostery in Hsp70 chaperones is transduced by subdomain rotations;Bhattacharya;J. Mol. Biol.,2009

3. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release;Bimston;EMBO J.,1998

4. Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein;Briknarová;Nat. Struct. Biol.,2001

5. BAG4/SODD protein contains a short BAG domain;Briknarová;J. Biol. Chem.,2002

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