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Related Concept Videos

Cooperative Allosteric Transitions01:58

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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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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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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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Related Experiment Video

Updated: May 1, 2026

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Dimerization-based control of cooperativity.

Mehdi Bouhaddou1, Marc R Birtwistle

  • 1Icahn School of Medicine at Mount Sinai, Department of Pharmacology and Systems Therapeutics, New York, NY 10029, USA. marc.birtwistle@mssm.edu.

Molecular Biosystems
|April 17, 2014
PubMed
Summary
This summary is machine-generated.

Dimerization, a common biological process, significantly controls how ligand-receptor binding cooperativity functions, sometimes overriding traditional affinity-based mechanisms. This suggests dimerization is key to tuning biological system responses.

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Area of Science:

  • Biochemistry
  • Systems Biology
  • Molecular Biology

Background:

  • Cooperativity in ligand-receptor binding is crucial for biochemical system function.
  • Traditionally, cooperativity is explained by changes in binding affinity after initial ligand binding.

Purpose of the Study:

  • To investigate the role of dimerization in modulating ligand-receptor binding cooperativity.
  • To determine if dimerization can influence or even dominate canonical allosteric mechanisms.

Main Methods:

  • Developed a general kinetic model for signal-mediated dimerization.
  • Performed exhaustive parameter sensitivity analysis on the model.

Main Results:

  • Dimerization can reinforce, eliminate, or reverse cooperativity driven by binding affinity.
  • The accumulation of stoichiometrically asymmetric dimers (1:2 ligand:receptor) is a key factor in dimerization-based cooperativity control.
  • The impact of asymmetric dimers on cooperativity is highly system-dependent.

Conclusions:

  • Dimerization offers a novel mechanism for generating and tuning cooperativity in biological systems.
  • The canonical allosteric model of cooperativity is incomplete without considering dimerization.
  • Dimerization's pervasive nature suggests a significant role in diverse biological functions.