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The Effects of Tryptophan 393 Point Mutation on Estrogen Receptor α BHPI Binding
Author(s) -
Bean Monica,
Livezey Mara
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.02719
Subject(s) - point mutation , tryptophan , mutation , estrogen receptor , chemistry , estrogen , medicine , genetics , endocrinology , biology , biochemistry , gene , amino acid , cancer , breast cancer
BHPI is a small molecule bio‐modulator of estrogen receptor α (ERα), which can result in the depletion of ATP, and ultimately necrotic cell death. Through activation of the anticipatory Unfolded Protein Response (aUPR) this potent drug blocks the proliferation of cancer cells. The purpose of this experiment was to determine how a tryptophan 393 point mutation to alanine would affect the binding of BHPI to a variety of ERα Protein Data Bank (PDB) structures—1a52, 3ert, and 5u2b, and to determine the most common BHPI binding sites on each of these structures, through using the following computational software: SwissDock, MolProbity, PyMOL, and refineD.