Related Experiment Video

Updated: Dec 12, 2025

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

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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Structural Insights into the Specificity of Ligand Binding and Coactivator Assembly by Estrogen-Related Receptor β

Benqiang Yao1, Shuchi Zhang1, Yijuan Wei1

  • 1The State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Fujian 361005, China.

Journal of Molecular Biology
|August 16, 2020
PubMed

Insights

Researchers solved the structure of Estrogen-related receptor beta (ERRβ) using a novel mutation for protein stability. This breakthrough enables new drug designs for ERR-mediated diseases.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Endocrinology

Background:

  • Estrogen-related receptor beta (ERRβ) is a crucial nuclear receptor with significant biological and pharmaceutical relevance.
  • The ERRβ ligand-binding domain structure remained unsolved, hindering research into nuclear receptor structures.

Purpose of the Study:

  • To overcome challenges in obtaining stable and soluble ERRβ protein for structural and biochemical studies.
  • To elucidate the structural basis of ERRβ function and its interactions.

Main Methods:

  • Identification of a single-residue mutation to enhance protein solubility and stability.
  • X-ray crystallography to determine the 3D structure of the ERRβ ligand-binding domain.

Main Results:

  • A robustly soluble and stable active ERRβ ligand-binding domain was successfully produced.
  • The crystal structure revealed key features enabling signal transduction analysis across all ERR subtypes.
  • The structure provides insights into ligand binding and coregulator recruitment mechanisms.

Conclusions:

  • The engineered ERRβ protein facilitates unprecedented biochemical and structural investigations.
  • The determined structure offers a framework for designing selective and potent drugs targeting ERR-mediated diseases.
Keywords:
coactivator bindingcrystal structuresligand recognitionnuclear receptor ERRβtranscriptional regulation

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