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Updated: Dec 13, 2025
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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
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Monitoring ligand-mediated helix 12 transitions within the human estrogen receptor α using bipartite tetracysteine
Ranju Pokhrel1, Tang Tang, Justin M Holub
1Department of Chemistry and Biochemistry, Ohio University, Athens, OH 45701, USA.
Organic & Biomolecular Chemistry
|July 30, 2020
Abstract:
Estrogen receptor α ligand-binding domains (ERα-LBD) expressing tetracysteine motifs bind FlAsH-EDT2 upon transition of helix 12 (H12) to a folded state. Changes in fluorescence intensity allowed surveillance of ligand-mediated H12 transitions and facilitated the determination of FlAsH association rates (kon) and apparent equilibrium dissociation constants (Kapp) to ERα-LBDs in the presence of estrogenic ligands.
