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Related Experiment Video

Updated: Jun 21, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
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Analysis of oestrogen receptor dimerisation using chimeric proteins.

R White1, S E Fawell, M G Parker

  • 1Molecular Endocrinology Department, Imperial Cancer Research Fund, London, England.

The Journal of Steroid Biochemistry and Molecular Biology
|January 1, 1991
PubMed
Summary
This summary is machine-generated.

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Researchers identified key sequences for estrogen receptor dimerization. Substituting regions from androgen and retinoic acid receptors reduced DNA binding, suggesting intramolecular incompatibility in nuclear hormone receptors.

Area of Science:

  • Molecular Biology
  • Endocrinology
  • Genetics

Background:

  • The hormone binding domain (HBD) of nuclear receptors plays a crucial role in receptor function, including dimerization and DNA binding.
  • Conserved residues within the HBD suggest potential functional compatibility across different nuclear hormone receptor superfamily members.

Purpose of the Study:

  • To identify sequences critical for dimerization within the mouse estrogen receptor's HBD.
  • To investigate the functional compatibility of the dimerization domain across different nuclear hormone receptors.
  • To analyze the impact of substituting regions from androgen and retinoic acid receptors into the estrogen receptor's dimerization domain.

Main Methods:

  • Insertional and point mutagenesis were used to identify essential dimerization sequences in the mouse estrogen receptor.

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Identification of Functional Protein Regions Through Chimeric Protein Construction
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Last Updated: Jun 21, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
09:16

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

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

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Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

  • Peptide sequences from human androgen receptor and retinoic acid receptor HBDs were substituted into the mouse estrogen receptor.
  • Gel retardation assays were employed to analyze high-affinity DNA binding of the resulting chimeric proteins.

    • Main Results:

    • Specific sequences essential for dimerization were identified in the mouse estrogen receptor HBD.
    • Chimeric estrogen receptors with substituted androgen or retinoic acid receptor sequences exhibited reduced DNA binding affinity compared to wild-type estrogen receptor.
    • The observed reduction in DNA binding suggests potential intramolecular incompatibilities within the HBD of nuclear hormone receptors.

    Conclusions:

    • Dimerization sequences within the estrogen receptor HBD are crucial for high-affinity DNA binding.
    • Functional compatibility of the dimerization domain is limited between different nuclear hormone receptors, as evidenced by reduced DNA binding in chimeric proteins.
    • Intramolecular interactions within the HBD may dictate functional compatibility and DNA binding efficiency across the nuclear hormone receptor superfamily.