Fig. 1
From: Role of HSF1 in cell division, tumorigenesis and therapy: a literature review
Schematic representation of the domain structure of human heat shock factor 1 (HSF1) [23]. The N-terminal DNA-binding domain enables interaction with heat shock elements (HSEs) in target gene promoters, with binding affinity significantly enhanced upon trimerization. Trimerization is driven by hydrophobic heptad repeats A, B, and C (HR-A/B/C). The transactivation domain (TAD) promotes transcriptional activation of heat shock genes, while its activity is modulated by the regulatory domain (RD)