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Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase
Abstract
The inadvertent activation of the Abelson tyrosine kinase (Abl) causes chronic myelogenous leukemia (CML). A small-molecule inhibitor of Abl (STI-571) is effective in the treatment of CML. We report the crystal structure of the catalytic domain of Abl, complexed to a variant of STI-571. Critical to the binding of STI-571 is the adoption by the kinase of an inactive conformation, in which a centrally located “activation loop” is not phosphorylated. The conformation of this loop is distinct from that in active protein kinases, as well as in the inactive form of the closely related Src kinases. These results suggest that compounds that exploit the distinctive inactivation mechanisms of individual protein kinases can achieve both high affinity and high specificity.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
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Metadata
- Authors
- Schindler, T., Bornmann, W., Pellicena, P., Miller, W. T., Clarkson, B., & Kuriyan, J.
- Venue
- Science
- Published
- 2000-09-15
- Volume
- 289
- Issue
- 5486
- Pages
- 1938-1942
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2131174104
- Cited by
- 1,780
- References
- 1
- FWCI
- 27.83
- Type
- journal article
- Language
- en
- Open access
- closed
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- Schindler, T., Bornmann, W., Pellicena, P., Miller, W. T., Clarkson, B., & Kuriyan, J. (2000). Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase. Science. https://doi.org/10.1126/science.289.5486.1938
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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