Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes

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.