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

Allosteric Regulation01:08

Allosteric Regulation

64.6K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
64.6K
Allosteric Regulation01:08

Allosteric Regulation

16.3K
16.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

9.4K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
9.4K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.8K
2.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.2K
3.2K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

6.0K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
6.0K

You might also read

Related Articles

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

Sort by
Same author

A unified catalytic mechanism in bifunctional DNA glycosylases with an evolutionarily conserved aspartate-lysine dyad.

Nature communications·2026
Same author

Deep mutational scanning of SARS-CoV-2 nucleocapsid reveals regional stability patterns.

Protein science : a publication of the Protein Society·2026
Same author

Endurance exercise elicits temporal and sexual dimorphic multi-omics remodeling of liver metabolism revealed by MoTrPAC.

Cell reports·2026
Same author

Immunological imprinting shapes the cross-reactive antibody responses to the KP.2 and LP.8.1 vaccine doses.

bioRxiv : the preprint server for biology·2026
Same author

Orchestrated metal ion repositioning defines the dynamic catalytic strategy of the essential DNA repair nuclease APE1.

bioRxiv : the preprint server for biology·2026
Same author

Subsets of adjacent nodes (SOAN): A fast method for computing suboptimal paths in protein dynamic networks.

Molecular physics·2026

Related Experiment Video

Updated: Mar 30, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K

Unexpected Allosteric Network Contributes to LRH-1 Co-regulator Selectivity.

Paul M Musille1, Bradley R Kossmann2, Jeffrey A Kohn1

  • 1From the Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322 and.

The Journal of Biological Chemistry
|November 11, 2015
PubMed
Summary

Phospholipids signal through the liver receptor homolog-1 (LRH-1) via an allosteric pathway. This study reveals how phospholipid structure dictates co-regulator interaction, offering insights into metabolic disease targets.

Keywords:
allosteric regulationdiabeteslipidsmolecular dynamicsnuclear receptorphosphatidylcholine

More Related Videos

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

9.6K
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

13.2K

Related Experiment Videos

Last Updated: Mar 30, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K
A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

9.6K
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

13.2K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Phospholipids (PLs) are unusual signaling hormones.
  • The nuclear receptor liver receptor homolog-1 (LRH-1) controls lipid and cholesterol homeostasis.
  • LRH-1 is a potential therapeutic target for metabolic and neoplastic diseases.

Purpose of the Study:

  • To elucidate the molecular mechanism linking phospholipid structure to transcriptional co-regulator preference in LRH-1.
  • To understand how structural dynamics in LRH-1's alternate activation function (AF) region influence co-regulator selectivity.
  • To identify the allosteric network connecting PL binding to co-regulator interaction.

Main Methods:

  • X-ray crystallography
  • Molecular modeling
  • Structural studies

Main Results:

  • Identified an unexpected allosteric network linking the alternate AF region and the canonical AF2 domain.
  • Demonstrated that communication between these regions is correlated with co-regulator interaction strength.
  • Observed that PL binding induces structural fluctuations in the alternate AF region.

Conclusions:

  • PLs activate LRH-1 through a novel allosteric pathway involving conformational dynamics.
  • The identified allosteric network dictates co-regulator selectivity based on PL structure.
  • This research provides the first insight into PL-mediated nuclear hormone receptor activation dynamics.