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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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 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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Updated: May 29, 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

Binding leverage as a molecular basis for allosteric regulation.

Simon Mitternacht1, Igor N Berezovsky

  • 1Computational Biology Unit/UNI Research, University of Bergen, Bergen, Norway.

Plos Computational Biology
|September 22, 2011
PubMed
Summary
This summary is machine-generated.

Binding leverage quantifies how well a binding site connects to protein motions. This metric helps predict functional sites and potential drug targets by analyzing protein dynamics.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Allosteric regulation is mediated by effector molecules inducing protein conformational changes.
  • Understanding protein dynamics is crucial for identifying functional and regulatory sites.

Purpose of the Study:

  • Introduce and define 'binding leverage' as a measure of site-motion coupling.
  • Evaluate the utility of binding leverage in identifying functional sites across various proteins.
  • Explore implications for predicting allosteric sites and drug design.

Main Methods:

  • Utilized Monte Carlo simulations to identify potential binding sites.
  • Employed normal modes and crystal structure pairs to model protein dynamics.
  • Analyzed catalytic domains and multimeric allosteric enzymes.

Main Results:

  • Identified high binding leverage for both catalytic and allosteric sites in most analyzed proteins.
  • Demonstrated that allosteric regulation without conformational change involves different motions.
  • Binding leverage can be calculated from a single crystal structure.

Conclusions:

  • Protein dynamics are essential for predicting functional sites.
  • Binding leverage offers a novel approach for characterizing proteins and identifying allosteric sites.
  • This method has significant implications for drug discovery and design.