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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...

Allosteric Regulation

Allosteric Regulation

Enzyme Inhibition

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

Inhibition of Cdk Activity

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...

Inhibition of CDK Activity

Inhibition of CDK Activity

Targets for Drug Action: Overview

Targets for Drug Action: Overview

Drugs target macromolecules to modify ongoing cellular processes. Primary drug targets include receptors, ion channels, transporters, and enzymes.
Receptors are either membrane-spanning or intracellular proteins, which upon binding a ligand, get activated and transmit the signal downstream to elicit a response. Drugs bind receptors, either mimicking the action of endogenous ligands or blocking the receptor activity to bring about a modified response. Nearly 35% of approved drugs target the G...

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Related Experiment Video

Updated: Mar 31, 2026

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

Published on: October 23, 2019

Allosteric small-molecule kinase inhibitors.

Peng Wu¹, Mads H Clausen², Thomas E Nielsen³

¹Department of Chemistry, Technical University of Denmark, Kgs. Lyngby DK-2800, Denmark.

Pharmacology & Therapeutics

|October 20, 2015

Summary

Targeting allosteric pockets offers a promising alternative to traditional kinase inhibitors for treating diseases like cancer. This approach enhances selectivity and overcomes drug resistance, with several allosteric inhibitors now in clinical trials.

Keywords:

Allosteric inhibitors MEK inhibitors Serine/threonine kinase Type III inhibitors Type IV inhibitors Tyrosine kinase

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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Area of Science:

Pharmacology and Drug Discovery
Molecular Biology and Biochemistry

Background:

Small-molecule kinase inhibitors are crucial targeted therapies, particularly for cancer.
Conventional inhibitors targeting the ATP-binding pocket face challenges in selectivity due to conserved kinase structures.
Drug resistance is a significant limitation of current ATP-competitive kinase inhibitors.

Purpose of the Study:

To explore allosteric kinase inhibition as a strategy to overcome selectivity and resistance issues.
To review the current understanding of allosteric inhibition, including its concepts, classifications, and advantages.
To highlight recent advancements and newly identified allosteric inhibitors from the past three years.

Main Methods:

Literature review and synthesis of current knowledge on allosteric kinase inhibition.
Analysis of approved and investigational allosteric kinase inhibitors.
Discussion of the conceptual framework, classification, and therapeutic potential of allosteric inhibitors.

Main Results:

Allosteric inhibition presents a viable alternative to ATP-pocket targeting, offering improved selectivity and potential to overcome resistance.
The field has seen significant progress, including the FDA approval of trametinib and over 10 other allosteric inhibitors in clinical trials.
A growing pipeline of selective and potent preclinical allosteric kinase inhibitors demonstrates the field's momentum.

Conclusions:

Allosteric kinase inhibition is an emerging and promising therapeutic strategy.
Further research and development in allosteric inhibitors are crucial for advancing targeted therapies.
This approach holds potential for improved treatment outcomes in various diseases, especially cancers.