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Updated: Oct 9, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
Estrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding
M Ruff1, M Gangloff, J M Wurtz
1IGBMC, UPR de biologie et génomique structurale, 1 Rue Laurent Fries, 67404 Illkirch, France. ruff@igbmc.u-strasbg.fr
Abstract:
Estrogen receptors are members of the nuclear receptor steroid family that exhibit specific structural features, ligand-binding domain sequence identity and dimeric interactions, that single them out. The crystal structures of their DNA-binding domains give some insight into how nuclear receptors discriminate between DNA response elements. The various ligand-binding domain crystal structures of the two known estrogen receptor isotypes (alpha and beta) allow one to interpret ligand specificity and reveal the interactions responsible for stabilizing the activation helix H12 in the agonist and antagonist positions.
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