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

64.2K
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...
64.2K
Allosteric Regulation01:08

Allosteric Regulation

16.1K
16.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

9.3K
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...
9.3K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

2.8K
2.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

3.2K
3.2K
The Two-State Receptor Model01:29

The Two-State Receptor Model

3.4K
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...
3.4K

You might also read

Related Articles

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

Sort by
Same author

Low Agonism and Balanced Pathway Modulation Distinguish an M1 Muscarinic Receptor Positive Allosteric Modulator Lacking Cholinergic Adverse Effects.

ACS chemical neuroscience·2026
Same author

Reimagining pharmacology education.

Pharmacological reviews·2026
Same author

The Concise Guide to PHARMACOLOGY 2025/26: G protein-coupled receptors.

British journal of pharmacology·2025
Same author

Structure-guided allosteric modulation of the delta opioid receptor.

bioRxiv : the preprint server for biology·2025
Same author

Dissociation kinetics of G proteins from G protein-coupled receptors and effects of allosteric modulation.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Structure-Activity Relationships of Highly Potent and Selective A<sub>2B</sub> Adenosine Receptor Agonists.

Journal of medicinal chemistry·2025

Related Experiment Video

Updated: Mar 15, 2026

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
07:16

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission

Published on: August 16, 2018

14.3K

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation.

Jean-Pierre Changeux1, Arthur Christopoulos2

  • 1Collège de France and CNRS URA 2182, Institut Pasteur, 75015 Paris, France.

Cell
|August 28, 2016
PubMed
Summary

Cells use four main receptor families to sense their environment. These allosteric proteins share common mechanisms for signal transition, offering new therapeutic possibilities.

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
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

Related Experiment Videos

Last Updated: Mar 15, 2026

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
07:16

Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission

Published on: August 16, 2018

14.3K
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
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

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Signaling
  • Drug Discovery

Background:

  • Four major receptor families (ligand- and voltage-gated ion channels, G-protein-coupled receptors, nuclear hormone receptors, receptor tyrosine kinases) mediate cellular responses to environmental signals.
  • These receptors are allosteric proteins characterized by multiple, conformationally linked ligand-binding sites.

Purpose of the Study:

  • To explore common mechanisms governing allosteric transitions in major receptor families.
  • To highlight the potential of synthetic allosteric modulators in therapeutic development.

Main Methods:

  • Review of recent studies on receptor allosteric mechanisms.
  • Analysis of factors influencing allosteric transitions, including oligomerization, conformational ensembles, disordered regions, and modulatory sites.

Main Results:

  • Identified common allosteric mechanisms across diverse receptor families.
  • Highlighted the role of oligomerization, conformational ensembles, intrinsically disordered regions, and allosteric modulatory sites in receptor function.
  • Noted the emergence of synthetic allosteric modulators for these receptors.

Conclusions:

  • Common allosteric principles govern the function of major cellular receptors.
  • Synthetic allosteric modulators represent a promising, albeit complex, avenue for novel therapeutics.