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. Author manuscript; available in PMC: 2019 Oct 15.
Published in final edited form as: Bioorg Med Chem. 2018 Apr 7;26(19):5299–5306. doi: 10.1016/j.bmc.2018.04.018

Figure 1.

Figure 1

Structure and molecular mechanisms of HSF1. (A) HSF1 is held in a repressed state through interactions between LZ1-3 and LZ4. A stress response leads to oligomerization and transcriptional activation of heat shock responsive genes. (B) Proposed mechanisms by which LZ1-3 or LZ4 derived peptides might mimic intra-molecular interactions and suppress HSF1 activation. This activity might be detected by a fluorescence polarization (FP) experiment, in which changes in binding of HSF1 to fluorescent HSE is measured. (C) Homology model of human HSF1 LZ1-3 domain homotrimer. Coiled-coils are shown in cartoon form (left and middle), while the peptide template for LZ1-3 ligand design is shown as a yellow cartoon (right).