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

Figure 3

Domain structure of human HSF1. DBD: DNA-binding domain (amino acids 1–110); HR-A/B: heptad repeat regions A and B (amino acids 130–203); RD: regulatory domain (amino acids 221–383). This domain negatively regulates the transactivating activity of HSF1; HR-C: heptad repeat region C (amino acids 384–409); TAD: transactivation domain (amino acids 410–529). HSF1 trimerizes through intermolecular interactions between the HR-A/B regions. Trimerization is negatively regulated by intramolecular interactions between the HR-A/B heptad repeat region and the HR-C domains within the monomer. The positions of the cysteine residues are indicated with yellow bars. The cysteine residues which participate in activating intermolecular disulfide bonds are shown in red, and those which participate in inactivating intramolecular disulfide bonds are shown in blue.