Fig. 5 | Signal Transduction and Targeted Therapy

Fig. 5

From: Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials

Fig. 5

The Hsp90/Cdc37 interactions and inhibitors. a Co-chaperone regulation of client protein activation. In the chaperone cycle of Hsp90, the open state Hsp90 firstly combined with HOP through its C terminal. Subsequently, it recruits Hsp40, Hsp70, client protein, and Cdc37 to form a mature complex. After ATP hydrolysis, ADP and mature client protein are released. Hsp90 is converted into an open state and enters the next ATP cycle. b The complex structure DCZ3112 and the N-terminal domain of Hsp90 modeled by molecular docking based on the crystal structure of Hsp90–Cdc37 complex (PDB:2K5B). c The chemical structures of inhibitors of Hsp90/Cdc37

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