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Transducer Mechanism: Nuclear Receptors

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:

Internal Receptors

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.

Intracellular Hormone Receptors

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

Types of Receptors: Internal Receptors

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...

Signal Transduction: Overview

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...

The Two-State Receptor Model

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...

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Related Experiment Video

Updated: May 10, 2026

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

Variable steroid receptor responses: Intrinsically disordered AF1 is the key.

S Stoney Simons¹, Raj Kumar

¹Steroid Hormones Section, NIDDK/LERB, National Institutes of Health, Bethesda, MD, United States. stoneys@helix.nih.gov

Molecular and Cellular Endocrinology

|June 25, 2013

Summary

Steroid hormones offer clinical benefits but cause side effects. Targeting the intrinsically disordered amino-terminal domain of steroid receptors could improve therapeutic selectivity and reduce adverse events.

Keywords:

A(max) and EC(50)AF1 domain as a molecular rheostat Intrinsically disordered domains Selective receptor modulators (SRMs)Selectivity in controlling gene expression Steroid receptors

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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

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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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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

Steroid hormones are widely used clinically to modulate gene expression via receptor proteins.
Current limitations in steroid therapy stem from uncontrolled off-target side effects.
Understanding steroid receptor mechanisms is crucial for developing safer treatments.

Purpose of the Study:

To integrate recent findings on steroid receptor structure and function.
To propose a novel framework for enhancing selectivity in steroid-based therapies.
To address the challenge of off-target effects in clinical steroid applications.

Main Methods:

Synthesizing data from studies on cofactor-induced structural changes in receptors.
Analyzing the impact of ligands on remote receptor regions.
Investigating the role of cofactor concentration in ligand potency and efficacy.

Main Results:

The intrinsically disordered amino-terminal domain is identified as a key determinant of receptor activity.
Ligand binding and cofactor interactions significantly influence receptor structure and function.
Cofactor concentration modulates both the potency and efficacy of steroid ligands.

Conclusions:

A novel framework integrating structural and functional data for steroid receptors has been developed.
This framework provides a basis for designing therapies with improved selectivity.
Targeting the amino-terminal domain offers a promising strategy to minimize side effects of steroid treatments.