Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

6.7K
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:
6.7K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

14.2K
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...
14.2K
Signal Transduction: Overview01:26

Signal Transduction: Overview

8.6K
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...
8.6K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.5K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.5K
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.9K
Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
4.9K
The Two-State Receptor Model01:29

The Two-State Receptor Model

3.5K
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...
3.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Conformational cycling of the Wntless transporter drives trafficking and secretion of Wnt morphogens.

Nature communications·2026
Same author

Prevalence and risk factors of latent tuberculosis infection among household contacts of tuberculosis patients: a cross-sectional study.

Frontiers in public health·2026
Same author

Advances in understanding aryl hydrocarbon receptor structure, function, and modulation.

Trends in biochemical sciences·2026
Same author

Structural insights into brain thyroid hormone transport via MCT8 and OATP1C1.

Cell·2025
Same author

Learning-based early detection of post-hepatectomy liver failure using temporal perioperative data: a nationwide multicenter retrospective study in China.

EClinicalMedicine·2025
Same author

Prospective multicenter validation of preoperative plasma ceramides as novel predictive biomarkers for clinically relevant post-hepatectomy liver failure.

International journal of surgery (London, England)·2025
Same journal

A Computational Systems Biology View on the Role of the Menstrual Cycle in Endocrine Health and Disease.

Journal of molecular endocrinology·2026
Same journal

Pancreatic β-cell aging in physiology and diabetes: emerging roles of m6A mRNA methylation.

Journal of molecular endocrinology·2026
Same journal

Neuroendocrine regulation of female fertility: the role of CNS-derived hormones.

Journal of molecular endocrinology·2026
Same journal

Hypothalamic neuropeptides as modulators of neural activity and behaviour.

Journal of molecular endocrinology·2026
Same journal

Massively parallel functional genomic assays in endocrinology: from promise to delivery.

Journal of molecular endocrinology·2026
Same journal

TSH promotes chemerin/CMKLR1-cAMP/ERK-DIO2 signaling in primary rat ependymal cells in vitro.

Journal of molecular endocrinology·2026
See all related articles

Related Experiment Video

Updated: May 7, 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

11.9K

Understanding nuclear receptor form and function using structural biology.

Fraydoon Rastinejad1, Pengxiang Huang, Vikas Chandra

  • 1Metabolic Signaling and Disease Program, Sanford-Burnham Medical Research Institute, Orlando, Florida 32827, USA.

Journal of Molecular Endocrinology
|October 10, 2013
PubMed
Summary
This summary is machine-generated.

Nuclear receptors (NRs) are key transcription factors. New structures reveal their full complex organization, improving understanding of signal transmission and drug discovery for NRs.

Keywords:
gene regulationmetabolismnuclear receptorssteroid hormonestranscription factors

More Related Videos

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K
Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

15.8K

Related Experiment Videos

Last Updated: May 7, 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

11.9K
Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

16.8K
Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
07:33

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

15.8K

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Nuclear receptors (NRs) are transcription factors that bind ligands to regulate gene expression.
  • Previous structural studies focused on isolated NR domains (LBDs, DBDs), revealing ligand/DNA binding and conformational states.
  • Understanding the coordinated function of entire NR complexes has been limited.

Purpose of the Study:

  • To investigate the higher-order quaternary architectures of NR complexes.
  • To elucidate the physical and functional coordination of NR polypeptide segments.
  • To provide frameworks for future drug discovery targeting NR signaling pathways.

Main Methods:

  • X-ray crystallography of NR heterodimers (PPARγ-RXRα) and homodimers (HNF-4α) bound to DNA.
  • Analysis of domain-domain interfaces within these complexes.
  • Structural comparison with previous studies of isolated NR domains.

Main Results:

  • Newly determined crystal structures reveal the higher-order organization of PPARγ-RXRα and HNF-4α complexes on DNA.
  • These structures highlight the complexity and uniqueness of domain-domain interfaces within NR complexes.
  • The findings provide insights into how signals are allosterically transmitted across different NR domains.

Conclusions:

  • Emerging structural data on NR complexes offer a more holistic view of their function.
  • These advances enhance our understanding of signal transduction in NRs.
  • The structural insights will guide the development of novel therapeutic agents targeting NR pathways.