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P324A Point Mutation as a Probe to Determine the Binding Site of BHPI on Estrogen Receptor Alpha

BHPI (1,3‐Dihydro‐3,3‐bis(4‐hydroxyphenyl)‐7‐methyl‐2H‐indol‐2‐one) is a noncompetitive bio‐modulator of estrogen receptor alpha (ERα) that induces necrotic cell death through ATP depletion and has shown promise as a preclinical anticancer drug. BHPI kills cancer cells through activating the anticipatory Unfolded Protein Response (aUPR). The UPR is a stress sensor within the endoplasmic reticulum that is normally a cytoprotective mechanism, but once hyperactivated by BHPI, leads to necrosis. Three ERα PDB structures 1a52, 3ert, and 5u2b were computationally analyzed with a Proline 324 to Alanine (P324A) point mutation to determine where and how BHPI binds to ERα. These studies are important for understanding the effects of amino acid mutations on protein‐ligand interaction, as well as the binding affinity of ERα for BHPI.