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. 2015 Jun 18;2015:301326. doi: 10.1155/2015/301326

Figure 1.

Figure 1

Overview of the HSP90 chaperone cycle. In the initial step, protein substrate bound to the HSP70-HSP40 chaperones interacts with HSP90; the formation of this complex is induced by HOP. ATP binding to HSP90 induces a conformation change in the complex, which leads to the substrate transfer from HSP70 to HSP90, and the release of the HSP70-HSP40 chaperones; the substrate-HSP90 complex is stabilized by p23 binding. Finally, the hydrolysis of ATP induces additional conformation changes leading to substrate release.