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

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:
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.
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

You might also read

Related Articles

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

Sort by
Same author

ERG orchestrates a dedifferentiation-senescence-inflammation triad in prostate cancer.

Molecular cancer research : MCR·2026
Same author

Associations of testosterone, sex hormone-binding globulin, and related hormones with risks of cancer death, incident cancer, and incident prostate cancer in men: individual participant data meta-analyses.

The lancet. Healthy longevity·2026
Same author

Polygenic risk score with KLK3 SNP-SNP interaction pairs for predicting prostate cancer aggressiveness.

Communications medicine·2026
Same author

Germline polygenic score for prostate cancer aggressiveness.

medRxiv : the preprint server for health sciences·2026
Same author

Oligometastatic prostate cancer - bridging the gap between localized and metastatic disease.

Nature reviews. Urology·2026
Same author

Case-Control and Longitudinal Study of Sex Steroids in Male Patients with CKD Before and After Kidney Transplantation.

Kidney international reports·2026
Same journal

Blood-based microRNAs as biomarkers of insulin resistance in childhood obesity: A systematic review and meta-analysis.

Molecular and cellular endocrinology·2026
Same journal

Female-specific metabolic genetic liability reveals a separable metabolic dimension of polycystic ovary syndrome.

Molecular and cellular endocrinology·2026
Same journal

The kisspeptin analog C6 elicits greater tachyphylaxis and transcriptional activation than kisspeptin-10 and -54.

Molecular and cellular endocrinology·2026
Same journal

G1 regulation of BK<sub>Ca</sub> channel leads to decreased migration of senescent pericytes and improved age-related hearing loss.

Molecular and cellular endocrinology·2026
Same journal

Maternal butyrate administration ameliorates fetal fatty liver and maternal metabolic alterations related to maternal obesity.

Molecular and cellular endocrinology·2026
Same journal

Retraction notice to " Steroid-induced oocyte maturation in Indian shad Tenualosa ilisha (Hamilton, 1822) is dependent on phosphatidylinositol 3 kinase but not MAP kinase activation" [Mol. Endocrinol. 390 (2014) 26-33].

Molecular and cellular endocrinology·2026
See all related articles

Related Experiment Video

Updated: May 30, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Structural basis for nuclear hormone receptor DNA binding.

Christine Helsen1, Stefanie Kerkhofs, Liesbeth Clinckemalie

  • 1Molecular Endocrinology Laboratory, Department Molecular Cell Biology, Campus GHB, ON1, Herestraat 49, 3000 Leuven, Belgium.

Molecular and Cellular Endocrinology
|August 2, 2011
PubMed
Summary
This summary is machine-generated.

Nuclear receptors bind DNA via conserved domains, with variations dictating specific gene targets. Receptor-specific DNA interactions and carboxy-terminal extensions fine-tune transcription and other cellular functions.

More Related Videos

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

Related Experiment Videos

Last Updated: May 30, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

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

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Nuclear receptors possess a conserved DNA-binding domain (DBD) crucial for gene regulation.
  • The DBD typically features zinc-coordinating modules that interact with DNA, often forming dimers on specific DNA sequences called hormone response elements (HREs).
  • HREs are composed of hexameric motifs arranged as direct, inverted, or everted repeats, influencing receptor binding modes (monomer, homodimer, heterodimer).

Purpose of the Study:

  • To elucidate the structural and functional basis of nuclear receptor DNA binding specificity.
  • To highlight the role of receptor-specific variations within the conserved DBD and associated regions in determining target gene regulation.
  • To explore how DNA-binding interactions influence other receptor functions beyond transcription.

Main Methods:

  • Bioinformatic analysis of conserved domains and sequence motifs in nuclear receptors.
  • Review of existing literature on nuclear receptor-DNA interactions and HRE structures.
  • Comparative analysis of DBD variations and their correlation with gene specificity.

Main Results:

  • Nuclear receptors exhibit conserved DBDs with variations that confer sequence specificity.
  • DNA-binding domains often dimerize on DNA, recognizing repeat hexamers in HREs.
  • The carboxy-terminal extension of the DBD plays a critical role in sequence specificity and other receptor functions like nuclear translocation and transactivation.

Conclusions:

  • Receptor-specific variations in DNA-binding domains and associated regions are key determinants of target gene selectivity.
  • DNA-binding elements can influence ligand-dependent receptor activity through allosteric signaling.
  • Understanding these intricate interactions is vital for comprehending nuclear receptor-mediated gene regulation.