Cross-Monomer Substrate Contacts Reposition the Hsp90 N-Terminal Domain and Prime the Chaperone Activity-Reference-Cited by-同舟云学术

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Cross-Monomer Substrate Contacts Reposition the Hsp90 N-Terminal Domain and Prime the Chaperone Activity

Published:2012-01 Issue:1 Volume:415 Page:3-15
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Street Timothy O.,Lavery Laura A.,Verba Kliment A.,Lee Chung-Tien,Mayer Matthias P.,Agard David A.

Funder

Howard Hughes Medical Institute

Damon Runyon Cancer Research Foundation

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference42 articles.

1. Hsp90: a specialized but essential protein-folding tool;Young;J. Cell Biol.,2001

2. Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone;Workman;Cancer Lett.,2004

3. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements;Shiau;Cell,2006

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

5. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90;Krukenberg;Structure,2008

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