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Related Concept Videos

Allosteric Proteins-ATCase01:19

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,...
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...
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...
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 9, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Allosite: a method for predicting allosteric sites.

Wenkang Huang1, Shaoyong Lu, Zhimin Huang

  • 1Department of Pathophysiology, Shanghai Jiao-Tong University School of Medicine, Shanghai 200025, China.

Bioinformatics (Oxford, England)
|July 12, 2013
PubMed
Summary
This summary is machine-generated.

Allosteric modulators offer therapeutic advantages over orthosteric ligands. A new tool, Allosite, aids in the computational prediction of allosteric sites for drug discovery.

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Area of Science:

  • Computational biology
  • Drug discovery
  • Protein structure analysis

Background:

  • Allosteric modulators present significant therapeutic advantages over orthosteric ligands, including enhanced specificity and reduced toxicity.
  • The precise prediction of allosteric sites is crucial for advancing drug discovery efforts.
  • Allosite is a novel computational tool designed for the automated prediction of allosteric sites in proteins.

Purpose of the Study:

  • To introduce Allosite, a new web server tool for predicting allosteric sites in proteins.
  • To facilitate the identification of potential allosteric drug targets.

Main Methods:

  • Development of an automated computational tool (Allosite) for allosteric site prediction.
  • Web server implementation for accessible use in protein analysis.

Main Results:

  • Allosite provides an automated method for predicting allosteric sites.
  • The tool is available as a web server, enhancing accessibility for researchers.

Conclusions:

  • Allosite represents a valuable new resource for the computational prediction of allosteric sites.
  • The tool can aid researchers in identifying novel therapeutic targets through allosteric modulation.