Review Article

The Role of Sulfhydryl Reactivity of Small Molecules for the Activation of the KEAP1/NRF2 Pathway and the Heat Shock Response

Figure 4

Domain structure of human Hsp90α. N-terminal domain (amino acids 1–209). This is the major site of ATP binding; L: flexible linker region (amino acids 210–271); MD: middle domain (amino acids 272–628) through which Hsp90 interacts with many of its client proteins; CTD: C-terminal domain (amino acids 629–732). Hsp90 forms a homodimer through the CTD. The positions of the cysteine residues are indicated with yellow bars. The most commonly modified cysteine residues by sulfhydryl-reactive small molecules are shown in red.
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