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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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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 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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Ligand Binding and Linkage00:49

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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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Allosteric Proteins-ATCase01:19

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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.
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Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
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On the Relationship Between Protein Stability, Thermostability, and Allosteric Signaling.

Raechell1, Wei-Ven Tee1, Bingxue Dong1

  • 1Bioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, #07-01, Matrix, Singapore 138671 Singapore.

Journal of Molecular Biology
|November 12, 2025
PubMed
Summary
This summary is machine-generated.

Protein stability and allosteric regulation are linked, with thermal adaptation shaping protein structure and sequence-determining allosteric signaling. Mutations impact fitness through complex epistasis beyond simple stability changes.

Keywords:
allosteric mutationsallosteryprotein dynamicsprotein stabilitythermostability

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Area of Science:

  • Protein biophysics
  • Structural biology
  • Systems biology

Background:

  • Protein thermodynamic stability and functional regulation are explained by the energy landscape framework.
  • Stability involves a native conformational ensemble, while function relies on transitions between states.
  • Allosteric regulation is driven by dynamics and conformational changes.

Purpose of the Study:

  • Investigate the relationship between protein structural stability and dynamics-driven allosteric regulation.
  • Identify general proteomic trends and specific determinants of protein stability.
  • Explore how stability and thermal adaptation influence protein structure and allosteric signaling.

Main Methods:

  • Analysis of general proteomic trends.
  • Investigation of fold/function-specific stability determinants.
  • Utilized a sequence-dependent model of allostery implemented in the AlloSigMA 3 web-server.
  • Studied inorganic pyrophosphatase, β-glucosidase, CheY, and adenylate kinase from various organisms.
  • Examined allosteric effects of mutations on protein fitness and bacterial growth rates.

Main Results:

  • Demonstrated an intricate relationship between protein stability and allosteric regulation.
  • Showed that stability and thermal adaptation shape protein structure.
  • Identified sequence-structure determinants controlling allosteric signaling.
  • Allosteric mutation effects in adenylate kinase correlated with observed changes in bacterial growth rates.
  • Observed epistasis, leading to non-additive fitness changes unexplained by stability alone.

Conclusions:

  • Protein stability and allosteric regulation are fundamentally interconnected.
  • Structural platform is shaped by stability requirements and thermal adaptation.
  • Allosteric signaling and regulation are controlled by sequence-structure determinants.
  • Epistasis plays a significant role in the effects of mutations on fitness.
  • The AlloSigMA 3 web-server provides tools for further investigation of stability-signaling relationships.