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Related Experiment Video

Updated: May 10, 2026

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

Crystal structures of ASK1-inhibtor complexes provide a platform for structure-based drug design.

Onkar Singh¹, Anthony Shillings, Peter Craggs

¹GlaxoSmithKline, Gunnels Wood Road, Stevenage, Hertfordshire, SG1 2NY, United Kingdom.

Protein Science : a Publication of the Protein Society

|June 19, 2013

Summary

A new

Keywords:

ASK1 apoptosis signal regulating kinase 1 structure base drug design

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Last Updated: May 10, 2026

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

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Area of Science:

Biochemistry
Structural Biology
Drug Discovery

Background:

Apoptosis signal-regulating kinase 1 (ASK1) is implicated in cancer, neurodegeneration, and cardiovascular diseases.
ASK1 is a promising drug target due to its role in various pathologies.

Purpose of the Study:

To develop a high-throughput method for determining the X-ray structures of ASK1/ligand complexes.
To investigate the binding site of ASK1 and its capacity to accommodate diverse ligands.

Main Methods:

A novel 'replacement-soaking' technique was employed for X-ray structure determination.
Five ASK1/ligand complexes from three different chemotypes were analyzed.

Main Results:

The replacement-soaking method enabled high-throughput structure determination of ASK1 complexes.
The ASK1 ATP binding site demonstrated adaptability to various chemical structures and binding modes.
The system accommodated protein flexibility, crucial for drug design.

Conclusions:

The developed crystal system is a robust platform for ASK1/ligand structure determination.
This method facilitates structure-based drug design for ASK1-targeting therapeutics.