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Cooperative Allosteric Transitions

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 Transitions

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 Transitions

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...

Allosteric Regulation

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 Regulation

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 Proteins-ATCase

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

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Updated: Jun 7, 2026

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

Exploring and exploiting allostery: Models, evolution, and drug targeting.

Alessio Peracchi¹, Andrea Mozzarelli

¹Department of Biochemistry and Molecular Biology, University of Parma, Parma, Italy. alessio.peracchi@unipr.it

Biochimica Et Biophysica Acta

|November 2, 2010

Summary

This summary is machine-generated.

Allostery, a key protein regulation mechanism, involves ligand binding at one site altering distant functions by exploiting protein flexibility. This fundamental biological process is now crucial for developing targeted allosteric drugs.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Allostery, conceptualized 50 years ago, explains how ligand binding at one site influences distant protein functions.
This mechanism relies on protein flexibility and energy landscape modulation, applicable to both monomeric and oligomeric proteins.

Purpose of the Study:

To review the fundamental principles and broad applications of allostery in biological regulation.
To highlight the evolutionary basis and therapeutic potential of allosteric mechanisms.

Main Methods:

Review of established theoretical models and experimental investigations of allosteric systems.
Analysis of evolutionary pressures shaping allosteric features in macromolecules.

Main Results:

Allostery is a fundamental regulatory mechanism across all life forms, impacting diverse processes like metabolism, receptor function, and cell motility.
Evolutionary studies reveal the selection and adaptation of allosteric traits in specific macromolecular systems.

Conclusions:

Allosteric regulation is a pervasive and fundamental biological process with significant implications for understanding protein function.
The exploitation of allosteric sites for drug development offers novel therapeutic strategies, enabling modulation of protein function for disease treatment.