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Updated: Oct 10, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
Structural insights into the mechanisms of agonism and antagonism in oestrogen receptor isoforms
R E Hubbard1, A C Pike, A M Brzozowski
1Structural Biology Laboratory, Chemistry Department, University of York, YO10 5DD, York, UK. rod@ysbl.york.ac.uk
Abstract:
Here we summarise the results that have emerged from our structural studies on the oestrogen receptor (ER) ligand-binding domain. We have investigated the conformational effects of a variety of ligands on the structures of both ER isoforms. Each class of ligand (agonists, partial agonists and selective oestrogen receptor modulators) induces a unique conformation in the receptor's ligand-dependent transcriptional activation function. Together these studies have broadened our understanding of ER function by providing a unique insight into ER's ligand specificity and the structural changes that underlie receptor agonism and antagonism.
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