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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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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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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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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Related Experiment Video

Updated: Sep 12, 2025

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Harnessing Allostery to Modulate Protein-Protein Interactions: From Function to Therapeutic Innovations.

Sutanu Mukhopadhyay1, Krishnendu Sinha1, Suman Chakrabarty1

  • 1Department of Chemical and Biological Sciences, S. N. Bose National Centre for Basic Sciences, Salt Lake, JD Block, Sector 3, Bidhan Nagar, Kolkata, West Bengal 700106, India.

Journal of Molecular Biology
|August 10, 2025
PubMed
Summary
This summary is machine-generated.

Targeting protein-protein interactions (PPIs) is challenging. Allosteric regulation, identified computationally, offers a new therapeutic strategy for diseases linked to dysregulated PPIs.

Keywords:
MD simulationallosterydrug designprotein–protein interactionssignaling

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Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Drug Discovery

Background:

  • Protein-protein interactions (PPIs) are crucial for cellular functions, but their dysregulation is implicated in many diseases.
  • Directly targeting PPIs is difficult due to their complex interfaces, often considered 'undruggable'.

Purpose of the Study:

  • To provide a comprehensive analysis of allosteric mechanisms in PPIs.
  • To highlight advances in computational identification and targeting of allosteric modulators.
  • To outline challenges and opportunities in developing allosteric therapies for PPIs.

Main Methods:

  • Review of recent advances in computational methodologies, including enhanced molecular dynamics simulations and machine learning.
  • Analysis of strategies for identifying and characterizing cryptic allosteric sites and pathways.
  • Examination of therapeutic interventions targeting allosteric sites.

Main Results:

  • Allosteric regulation provides a viable alternative to directly targeting PPIs by modulating function via distinct regulatory sites.
  • Computational tools have significantly improved the identification of allosteric sites and pathways.
  • Recent successes demonstrate the potential of targeting allosteric modulators.

Conclusions:

  • Allosteric modulation represents a promising therapeutic strategy for diseases involving dysregulated PPIs.
  • Translating computational insights into effective therapies requires addressing current challenges.
  • Targeting allosteric sites offers transformative potential for complex disease interventions.