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Cooperative Allosteric Transitions

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 Transitions

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Ligand Binding and Linkage

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...

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric Regulation

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...

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Related Experiment Video

Updated: Apr 18, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

A dynamically coupled allosteric network underlies binding cooperativity in Src kinase.

Zachariah H Foda¹, Yibing Shan², Eric T Kim²

¹Department of Pharmacological Sciences, Stony Brook University, Stony Brook, New York 11794, USA.

Nature Communications

|January 21, 2015

Summary

This summary is machine-generated.

Scientists discovered an allosteric network in Src kinase that controls its activity. This network reveals how protein tyrosine kinases (PTKs) regulate signals and may explain drug resistance.

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Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Protein tyrosine kinases (PTKs) are crucial drug targets due to their role in various human diseases.
Understanding how PTKs switch between active and inactive states is essential for drug development.
The precise mechanisms of signal integration within the kinase domain remain incompletely understood.

Purpose of the Study:

To identify the allosteric network connecting regulatory sites to catalytic sites in Src kinase.
To elucidate the binding cooperativity of substrates and products in Src kinase.
To explore the conservation of this allosteric network in other protein tyrosine kinases.

Main Methods:

Identification of an allosteric network of dynamically coupled amino acids in Src kinase.
Biochemical studies to confirm signal relay through the identified allosteric network.
Experimental analysis of two additional protein tyrosine kinases to assess network conservation.

Main Results:

An allosteric network connecting regulatory sites to ATP- and substrate-binding sites in Src kinase was identified.
Src kinase exhibits negative cooperativity for reactant binding (ATP, peptide) and positive cooperativity for product binding (ADP, phosphopeptide).
The allosteric network appears to be conserved across different protein tyrosine kinases.

Conclusions:

The study reveals a novel allosteric network governing protein tyrosine kinase regulation.
This network provides insights into kinase signal transduction and the mechanism of drug resistance.
Findings offer a potential target for overcoming resistance to ATP-competitive kinase inhibitors.