Abstract
Aurora kinases play an essential role in mitosis and cell cycle regulation. In recent years Aurora kinases have proved popular cancer targets and many inhibitors have been developed. The majority of these clinical candidates are multi-targeted, rendering them inappropriate as tools for studying Aurora kinase mediated signaling. Here we report discovery of a highly selective inhibitor of Aurora kinases A, B and C, with potent cellular activity and minimal off-target activity (PLK4). The X-ray co-crystal structure of Aurora A in complex with compound 2 is reported, and provides insights into the structural determinants of ligand binding and selectivity.
| Original language | English |
|---|---|
| Pages (from-to) | 4405-4408 |
| Number of pages | 4 |
| Journal | Bioorganic and Medicinal Chemistry Letters |
| Volume | 27 |
| Issue number | 18 |
| DOIs | |
| Publication status | Published - 2017 |
Bibliographical note
Funding Information:We would like to acknowledge funding from NIH R01 U54 HL127365 , the Linde center for chemical biology and the KU-KIST Graduate School of Converging Science and Technology Program.
Publisher Copyright:
© 2017 Elsevier Ltd
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This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Aurora kinase
- Cancer
- Mitosis
- Pan-Aurora inhibitor
- Selective kinase inhibitor
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry
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