Structural Studies of the Hsp90-Cdc37 Complex Using EPR Spectroscopy
نویسنده
چکیده
Hsp90 is a molecular chaperone, a vital protein that facilitates the folding and unfolding of a variety of proteins or ‘clients’. Kinases are one such client, with over half of the human kinome dependent on Hsp90 for activation (1). As its name suggests, Hsp90 is a heat shock protein and thus is highly expressed when the cell is under stress to ensure that proteins are folded and active. Its expression has also been found to be up to 10-fold greater in cancer cells (2), with many of Hsp90’s client kinases key players in oncogenic transformation. Despite its importance, the structural changes that enable Hsp90 to activate client are still unclear.
منابع مشابه
Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.
Hsp90 is an ATP-dependent molecular chaperone, which facilitates the activation and stabilization of hundreds of client proteins in cooperation with a defined set of cofactors. Many client proteins are protein kinases, which are activated and stabilized by Hsp90 in cooperation with the kinase-specific co-chaperone Cdc37. Other Hsp90 co-chaperones, like the ATPase activator Aha1, also are implic...
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