The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis-Reference-Cited by-同舟云学术

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The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis

Published:2012-07-13 Issue:8 Volume:21 Page:1162-1171
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Cunningham Christian N.,Southworth Daniel R.,Krukenberg Kristin A.,Agard David A.

Funder

UC Discovery Grant

NIH

ACS Postdoctoral Fellowship

NSDEG Graduate Fellowship

Howard Hughes Medical Institute

ARCS Fellowship

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2103/fullpdf

Reference45 articles.

1. Pathways of chaperone-mediated protein folding in the cytosol;Young;Nat Rev Mol Cell Biol,2004

2. Disassembly of transcriptional regulatory complexes by molecular chaperones;Freeman;Science,2002

3. Heat-shock protein 90, a chaperone for folding and regulation;Picard;Cell Mol Life Sci,2002

4. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery;Pratt;Exp Biol Med,2003

5. Coordinated ATP hydrolysis by the Hsp90 dimer;Richter;J Biol Chem,2001

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