… The requirement of Hsp90 for the function of oncogenic protein kinases such as ErbB2,
Cdk4, B-Raf and Akt/protein kinase B (reviewed in ref. 5) makes it an attractive target for new …

… The structural homology between the ATP-binding sites in gyrase B and Hsp90 suggests
that Glu33 might play a similar role in the ATPase activity of Hsp90. Thus, mutations of Asp79 …

… (B) Stereo pair secondary structure cartoon of the yeast Hsp90 middle segment, rainbow …
(B) Location of mutated residues on the middle segment structure. Residues in cyan are in the …

Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are
poorly defined. A ubiquitous family of stress-regulated proteins have been identified (Aha1, …

How the ATPase activity of Heat shock protein 90 (Hsp90) is coupled to client protein activation
remains obscure. Using truncation and missense mutants of Hsp90, we analysed the …

The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is
dependent on the binding and hydrolysis of ATP, and on interactions with a variety of co‐chaperones …

Recruitment of protein kinase clients to the Hsp90 chaperone involves the cochaperone p50
cdc37 acting as a scaffold, binding protein kinases via its N-terminal domain and Hsp90 via …

In vivo activation of client proteins by Hsp90 depends on its ATPase-coupled conformational
cycle and on interaction with a variety of co-chaperone proteins. For some client proteins …

… coli-expressed protein itself was unreactive, but developed a clear signal on incubation
with CK2 (Figure 1B), confirming the specific recognition of the phosphorylated Cdc37 by our …

… shown that Hsp90 is structurally and biochemically related to DNA-gyrase B and MutL ( …
Sti1 (A) and Sba1 (B) inhibition of the ATPase activity of Hsp90 ts-mutants showing that their …