Introduction
Hsp90 uses a host of cochaperones which not only regulate the ATPase activity and conformational dynamics but which also mediate interactions with Hsp90 client proteins.An hsp90 inhibitor usually binds to the ATP-binding pocket N-Terminal domain of hsp90, hence, blocks the binding of nucleotides to Hsp90. And some other inhibitors could bind at a second ATP-binding site in the C-terminal domain of Hsp90, thus disrupting the dimerization of the Hsp90 complex.
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