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Related Concept Videos

The Two-State Receptor Model01:29

The Two-State Receptor Model

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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...
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Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

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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:
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G Protein-coupled Receptors01:15

G Protein-coupled Receptors

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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.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
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Intracellular Hormone Receptors01:08

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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
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Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

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Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but...
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Types of Receptors: Internal Receptors01:07

Types of Receptors: Internal Receptors

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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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Related Experiment Video

Updated: Oct 15, 2025

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

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Structural insights into glucocorticoid receptor function.

Filipp Frank1, Eric A Ortlund1, Xu Liu1

  • 1Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, U.S.A.

Biochemical Society Transactions
|October 28, 2021
PubMed
Summary
This summary is machine-generated.

The glucocorticoid receptor (GR) regulates gene transcription for metabolism, stress, and inflammation. Structural studies reveal its interaction mechanisms, guiding improved anti-inflammatory drug design.

Keywords:
DNA binding domainglucocorticoid receptorligand binding domaintransactivationtransrepression

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Pharmacology

Background:

  • The glucocorticoid receptor (GR) is a key transcription factor regulating numerous genes.
  • GR activity is crucial for metabolism, development, stress, and inflammatory responses.
  • Structural insights into GR interactions have advanced understanding of its context-specific functions.

Purpose of the Study:

  • To summarize established and emerging mechanisms of GR action from a structural viewpoint.
  • To review how structural knowledge of GR function can inform future drug design.
  • To explore potential improvements in the therapeutic index of glucocorticoids for inflammatory disorders.

Main Methods:

  • Review of structural studies on GR interactions.
  • Analysis of GR domains and their roles in DNA and coregulator binding.
  • Discussion of intrinsically disordered regions in GR condensate formation.

Main Results:

  • Recent structural studies illuminate GR's complex interactions with ligands, DNA, and coregulators.
  • The intrinsically disordered region of GR plays a significant role in condensate formation.
  • Understanding these structural mechanisms provides a basis for targeted therapeutic interventions.

Conclusions:

  • Structural perspectives offer a deeper understanding of glucocorticoid receptor (GR) function.
  • Knowledge of GR structural mechanisms can guide the development of novel glucocorticoids.
  • Future glucocorticoid design may lead to improved treatments for inflammatory conditions with enhanced safety profiles.