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Related Concept Videos

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:
Signal Transduction: Overview01:26

Signal Transduction: Overview

Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
Intracellular Hormone Receptors01:08

Intracellular Hormone Receptors

Lipid-soluble hormones diffuse across the plasma and nuclear membrane of target cells to bind to their specific intracellular receptors. These receptors act as transcription factors that regulate gene expression and protein synthesis in the target cell
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.
Dose-Response Relationship: Selectivity and Specificity01:25

Dose-Response Relationship: Selectivity and Specificity

Drugs exert their therapeutic effects by interacting with receptors, enzymes, or ion channels that are present throughout the human body. The strength and duration of the interaction between a drug and its target receptor are characterized by the selectivity and specificity of the drug. Selectivity refers to a drug's strong preference for its intended target over other targets. For instance, isoprenaline, a non-selective β-adrenergic agonist, interacts with both β1- and β2-adrenergic receptors...
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.
Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...

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Updated: May 22, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
10:51

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 15, 2013

Ligand selectivity by nuclear hormone receptors.

J M Wurtz1, D Moras

  • 1a Laboratoire de Biologie Structurale , IGBMC, CNRS/INSERM/ULP/Collège de France , 1, rue Laurent Fries, BP 163 , 67404 , ILLKIRCH , France.

Journal of Biomolecular Structure & Dynamics
|May 22, 2012
PubMed
Summary

Analysis of nuclear receptor ligand binding domains reveals distinct structural features. Retinoic acid receptors (RAR) have rigid pockets, while estrogen receptors (ER) show greater flexibility in accommodating various ligands.

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Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
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Area of Science:

  • Structural Biology
  • Molecular Endocrinology
  • Biochemistry

Background:

  • Numerous crystal structures of nuclear receptor ligand binding domains (LBDs) are available.
  • Retinoic acid receptors (RAR) and estrogen receptors (ER) are well-characterized nuclear receptors with extensive agonist and antagonist complex data.

Purpose of the Study:

  • To analyze the key structural features of the RAR and ER ligand binding pockets (LBPs).
  • To understand the molecular basis of ligand selectivity in these nuclear receptors.

Main Methods:

  • Comparative analysis of known crystal structures of RAR and ER LBDs complexed with various ligands.
  • Examination of ligand-receptor interactions within the LBP.

Main Results:

  • The RAR LBD possesses a rigid architecture that dictates ligand adaptation.
  • The ER LBD demonstrates a flexible LBP capable of accommodating diverse ligand shapes and sizes.
  • These distinct LBP characteristics are crucial for receptor-specific ligand selectivity.

Conclusions:

  • Ligand binding pocket flexibility is a key determinant of nuclear receptor ligand selectivity.
  • RAR and ER LBDs exhibit contrasting structural strategies for ligand recognition and binding.