FIGURE 2.

HSP90 chaperone cycle. HSP90 chaperone undergoes dynamic cycling process, transitioning between open and closed states to promote maturation of polypeptide clients into functional proteins with the help of ATP and a variety of co‐chaperones. Targeting Hsp90 and its interaction with co‐chaperone could lead to the degradation of client proteins by 26S proteasome. HSP, heat shock protein; CDC37, co‐chaperone cell division cycle 37; HIP, the Hsp70‐interacting protein; Ub, ubiquitin; Pi, pyrophosphoric acid; N, NTD; M, MD; C, CTD; HOP, The Hsp70/Hsp90 organizing protein; Aha1, activator of heat shock 90 kDa protein ATPase homolog 1.