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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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...
Allosteric Regulation01:08

Allosteric Regulation

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...
Regulation of Metabolism01:19

Regulation of Metabolism

Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...

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Related Experiment Video

Updated: May 7, 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

The concept of allosteric modulation: an overview.

Jean-Pierre Changeux

    Drug Discovery Today. Technologies
    |September 21, 2013
    PubMed
    Summary

    This study reviews allosteric interactions in ligand-gated ion channels, identifying multiple modulation sites across different domains. These findings highlight new drug design targets and therapeutic opportunities.

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Neuroscience

    Background:

    • Allosteric interactions are crucial for regulating protein function.
    • Pentameric ligand-gated ion channels (LGICs) serve as a key model system for studying these interactions.

    Purpose of the Study:

    • To provide a historical overview of allosteric interaction concepts.
    • To identify and categorize different types of allosteric control in LGICs.
    • To explore potential drug design targets based on allosteric modulation.

    Main Methods:

    • Literature review and synthesis of historical and current research on allosteric modulation.
    • Analysis of allosteric sites within LGICs, including extracellular, transmembrane, and cytoplasmic domains.

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

    Published on: February 20, 2018

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

    Published on: August 16, 2018

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    Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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    Published on: October 4, 2024

    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

    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

    Main Results:

    • Recognition of diverse allosteric control mechanisms in LGICs over decades.
    • Identification of allosteric sites in extracellular (e.g., Ca2+, benzodiazepines), transmembrane (e.g., general anesthetics), and cytoplasmic domains.
    • Demonstration of multiple levels of allosteric modulation.

    Conclusions:

    • Allosteric modulation of LGICs offers multiple targets for therapeutic intervention.
    • Recent technological advancements present new opportunities for studying and exploiting allosteric mechanisms.
    • Understanding allosteric control is vital for advancing drug design in neuroscience and related fields.