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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

62.7K
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...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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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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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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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...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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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...
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Related Experiment Video

Updated: Jan 4, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

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Progress in Allosteric Database.

Kun Song1, Jian Zhang1, Shaoyong Lu2

  • 1Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University, School of Medicine, Shanghai, China.

Advances in Experimental Medicine and Biology
|November 11, 2019
PubMed
Summary
This summary is machine-generated.

Allosteric mechanisms regulate biological processes by transmitting signals between distant sites on macromolecules. The AlloSteric Database (ASD) provides integrated data on allosteric proteins, modulators, and pathways to advance research and drug discovery.

Keywords:
ASDAllosteryDrug development

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Allosteric mechanisms are crucial for biological regulation and drug development.
  • The understanding of allostery has evolved with new data and models over the past two decades.
  • The AlloSteric Database (ASD) has been a key resource for allosteric research since 2009.

Purpose of the Study:

  • To introduce the history and utility of the AlloSteric Database (ASD).
  • To highlight specific applications demonstrating the value of ASD in biological research.
  • To provide a comprehensive overview of allosteric proteins, modulators, sites, pathways, and networks.

Main Methods:

  • Review of the AlloSteric Database (ASD) architecture and content.
  • Case studies illustrating the application of ASD data in biological investigations.
  • Analysis of trends and advancements in allosteric research facilitated by ASD.

Main Results:

  • ASD serves as a comprehensive repository for diverse allosteric information.
  • The database has supported numerous studies in understanding allosteric mechanisms.
  • Specific examples showcase the practical benefits of using ASD for research and drug discovery.

Conclusions:

  • The AlloSteric Database (ASD) is an invaluable resource for the scientific community.
  • ASD facilitates deeper insights into allosteric regulation and its therapeutic potential.
  • Continued development and utilization of ASD will drive future advancements in allosteric research.