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M-Cdk Drives Transition Into Mitosis

M-Cdk Drives Transition Into Mitosis

Checkpoints throughout the cell cycle serve as safeguards and gatekeepers, allowing the cell cycle to progress in favorable conditions and slow or halt it in problematic ones. This regulation is known as the cell cycle control system.
Cyclin-dependent kinases, or Cdks, work in concert with cyclins to control cell cycle transitions. M-Cdk, a complex of Cdk1 bound to M cyclin, is a well-known example of this coordinated control that drives the transition from the G2 to the M phase.
M cyclin...

Positive Regulator Molecules

Positive Regulator Molecules

Mitotic cell division results in daughter cells that exactly resemble the parent cell. However, errors in the DNA replication or distribution of genetic material may lead to genetic mutations that may be passed down to every new cell formed from the resulting abnormal cell. Propagation of such mutant cells is restricted through checkpoint mechanisms present at different stages of the cell cycle. These checkpoints involve regulator molecules that either promote or demote cell cycle events.

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

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Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: May 27, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Cyclin-dependent kinases 5 template: useful for virtual screening.

Siripit Pitchuanchom¹, Chantana Boonyarat, Stefano Forli

¹Natural Products Research Unit, Department of Chemistry and Center for Innovation in Chemistry, Faculty of Science, Khon Kaen University, Khon Kaen, Thailand.

Computers in Biology and Medicine

|November 15, 2011

Summary

This summary is machine-generated.

This study created a Cyclin-Dependent Kinase 5 (Cdk5) active site template for structure-based drug design. The validated Cdk5 template accurately predicts inhibitor binding, aiding in the development of new therapeutics.

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Area of Science:

Biochemistry
Structural Biology
Medicinal Chemistry

Background:

Cyclin-Dependent Kinase 5 (Cdk5) is implicated in various neurological disorders.
Targeting the Cdk5 active site is a key strategy for developing novel therapeutics.
Accurate computational models are crucial for structure-based drug design.

Purpose of the Study:

To develop a reliable computational template of the Cdk5 active binding site.
To validate the template's accuracy in predicting ligand interactions.
To assess the template's utility in evaluating known Cdk5 inhibitors.

Main Methods:

Development of a Cdk5 active site template.
Validation using redocking of known ligands (PDB codes 1UNG, 1UNL, 1UNH).
Application of the template to predict binding modes and affinities of 36 known Cdk5 inhibitors.

Main Results:

The Cdk5 template demonstrated high accuracy, with docked ligand orientations matching crystallographic data (RMSD < 2.0Å).
The template effectively predicted ligand binding orientations and affinities.
Predicted binding energies for 36 inhibitors correlated well with their reported biological activities.

Conclusions:

The developed Cdk5 template serves as a robust model for structure-based drug design.
This template can accurately predict ligand binding, facilitating the discovery of new Cdk5 inhibitors.
The study highlights the potential of this model system for advancing Cdk5-targeted drug development.