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Updated: Jun 21, 2026
Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays
Published on: October 23, 2019
Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib
Navratna Vajpai1, André Strauss, Gabriele Fendrich
1Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, Switzerland.
Abstract:
Imatinib (Glivec or Gleevec) potently inhibits the tyrosine kinase activity of BCR-ABL, a constitutively activated kinase, which causes chronic myelogenous leukemia (CML). Here we report the first almost complete backbone assignment of c-ABL kinase domain in complex with imatinib.
Insights
Imatinib effectively blocks BCR-ABL kinase, the cause of chronic myelogenous leukemia (CML). This study provides the first near-complete structural assignment of the c-ABL kinase domain when bound to imatinib.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Chronic myelogenous leukemia (CML) is driven by the BCR-ABL tyrosine kinase.
- Imatinib is a potent inhibitor of BCR-ABL tyrosine kinase activity.
Purpose of the Study:
- To determine the structural basis of imatinib's inhibition of BCR-ABL.
- To provide a near-complete backbone assignment of the c-ABL kinase domain in complex with imatinib.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy was used.
- Assignment of the c-ABL kinase domain backbone was performed.
Main Results:
- A near-complete backbone assignment of the c-ABL kinase domain was achieved.
- The structural complex of c-ABL kinase domain with imatinib was characterized.
Conclusions:
- This structural data provides insights into imatinib's mechanism of action.
- Understanding the imatinib-BCR-ABL complex is crucial for CML treatment strategies.
