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Related Concept Videos

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.
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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:
Target Cell Response to Hormones01:22

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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Types of Receptors: Internal Receptors01:07

Types of Receptors: Internal Receptors

Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism.
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An Ex vivo Model to Study Hormone Action in the Human Breast
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Published on: January 8, 2015

Using thermodynamics to understand progesterone receptor function: method and theory.

Keith D Connaghan-Jones1, David L Bain

  • 1Department of Pharmaceutical Sciences, University of Colorado Denver, Denver, Colorado, USA.

Methods in Enzymology
|March 18, 2009
PubMed
Summary
This summary is machine-generated.

This study introduces a quantitative approach to understand progesterone receptor (PR) and coactivator assembly at gene promoters. It provides a framework for precise measurement of molecular interactions, advancing predictive models of receptor function.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Progesterone receptors (PRs) are nuclear receptors regulating gene transcription.
  • Current understanding of PR assembly and coactivator recruitment lacks quantitative predictive power.
  • Previous studies relied on qualitative or semi-quantitative methods, limiting insight into molecular interactions.

Purpose of the Study:

  • To develop and present an experimental and theoretical approach for dissecting PR and coactivator assembly at promoters.
  • To enable a quantitatively predictive understanding of progesterone receptor function.
  • To resolve microscopic interaction parameters and integrate them into a functional molecular code.

Main Methods:

  • Utilizing analytical ultracentrifugation for precise molecular characterization.
  • Employing quantitative DNase footprint titration to map protein-DNA interactions.
  • Coupling experimental data with exact theoretical treatments for robust analysis.

Main Results:

  • Demonstrated a method to experimentally dissect linked reactions in PR-coactivator assembly.
  • Provided a framework for resolving intrinsic binding constants and cooperativity terms.
  • Established a basis for integrating microscopic parameters into a functional molecular code.

Conclusions:

  • The developed approach offers a rigorous, quantitative method to study nuclear receptor function.
  • This quantitative framework is crucial for a predictive understanding of gene regulation by PR.
  • Findings necessitate a reevaluation of receptor function based on precise biophysical parameters.