Article
Biochemical and structural studies of the interaction of Cdc37 with Hsp90.
Journal of molecular biology - 16 Jul 2004
Zhang Wei, Hirshberg Miriam, McLaughlin Stephen H, Lazar Greg A, Grossmann J Günter, Nielsen Peter R, Sobott Frank, Robinson Carol V, Jackson Sophie E, Laue Ernest D
Abstract excerpt
The heat shock protein Hsp90 plays a key, but poorly understood role in the folding, assembly and activation of a large number of signal transduction molecules, in particular kinases and steroid hormone receptors. In carrying out these functions Hsp90 hydrolyses ATP as it cycles between ADP- and ATP-bound forms, and this ATPase activity is regulated by the transient association with a variety of co-chaperones....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.