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An intracellular conformational sensor assay for Abl T315I
Vicki Zhou1, Xiaoqi Gao, Shulin Han
1Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.
Analytical Biochemistry
|December 9, 2008
Summary
Researchers developed a novel high-throughput screening assay to monitor kinase conformations. This split luciferase sensor enables studying Abl kinase activity and inhibitors in cells.
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Kinase activity is regulated by conformational changes.
- Allosteric kinase inhibitors are valuable research tools and potential therapeutics.
- Current assays for monitoring kinase conformations are not suitable for high-throughput screening (HTS).
Purpose of the Study:
- To develop an HTS-compatible assay for monitoring kinase conformations.
- To create a cellular sensor for Abl kinase activity.
- To enable the discovery of novel kinase modulators.
Main Methods:
- Development of a split luciferase-based conformational sensor for Abl kinase.
- Utilizing intramolecular structural rearrangements to report on kinase activity.
- Employing a T334I Abl mutant for enhanced HTS suitability.
Main Results:
- The split luciferase sensor effectively monitors Abl kinase conformational changes in cells.
- The assay responds to both kinase deactivation and small molecule inhibition.
- The T334I Abl mutant is well-suited for HTS and inhibitor studies.
Conclusions:
- A novel HTS-compatible assay for monitoring kinase conformations has been established.
- This split luciferase approach provides a versatile tool for studying kinase biology.
- The method holds potential for broader application to other kinases and enzymes.