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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Internal Receptors01:31

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
Target Cell Response to Hormones01:22

Target Cell Response to Hormones

Hormones intricately bind to receptors on the surface or within target cells, initiating a cascade of cellular responses.
Notably, the cellular response can be regulated by altering the number of receptors expressed in the cell. For example, prolonged exposure to elevated hormone levels results in a gradual decline or down-regulation in the number of receptors for that specific hormone on the cell surface. Conversely, in response to low hormone levels, cells may use up-regulation, producing an...

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Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer
10:36

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Published on: March 17, 2016

Estrogen response elements function as allosteric modulators of estrogen receptor conformation

J R Wood1, G L Greene, A M Nardulli

  • 1Department of Molecular and Integrative Physiology, University of Illinois, Urbana 61801, USA.

Molecular and Cellular Biology
|April 7, 1998
PubMed
Summary

Estrogen receptor (ER) DNA binding differs between gene elements, influencing gene regulation. Understanding these interactions is key to modulating estrogen-responsive genes.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Endocrinology

Background:

  • Estrogen receptor (ER) is a transcription factor regulating gene expression.
  • ER binds to estrogen response elements (EREs) to mediate transcriptional changes.

Purpose of the Study:

  • To investigate the interaction of Xenopus laevis ER DNA binding domain (DBD) and intact ER with specific EREs.
  • To elucidate how differential ERE binding affects ER conformation and gene regulation.

Main Methods:

  • Gel mobility shift assays
  • DNase I footprinting
  • Methylation interference assays
  • Antibody supershift experiments
  • Protease digestion

Main Results:

  • ER DBD binding mode (monomer/dimer) varied depending on ERE sequence and concentration.
  • ER conformation differed upon binding to A2 and pS2 EREs, indicated by antibody and protease studies.
  • Differential ERE interaction leads to distinct ER conformational changes.

Conclusions:

  • Xenopus laevis ER exhibits sequence-specific DNA binding and conformational flexibility.
  • ERE-induced conformational changes in ER influence interactions with other transcription factors.
  • This mechanism facilitates differential regulation of estrogen-responsive genes.