Structures of the Cancer Related Aurora-A, FAK and EphA2 Protein Kinases from Nanovolume CrystallographyNowakowski, J., Cronin, C.N., McRee, D.E., Knuth, M.W., Nelson, C., Pavletich, N., Rogers, J., Sang, B.C., Scheibe, D.N., Swanson, R.V., Thompson, D.A.
(2003) Structure 10: 1659-1667
- PubMed: 12467573
- DOI: https://doi.org/10.1016/s0969-2126(02)00907-3
- Primary Citation of Related Structures:
1MP8, 1MQ4, 1MQB
- PubMed Abstract:
Protein kinases are important drug targets in human cancers, inflammation, and metabolic diseases. This report presents the structures of kinase domains for three cancer-associated protein kinases: ephrin receptor A2 (EphA2), focal adhesion kinase (FAK), and Aurora-A. The expression profiles of EphA2, FAK, and Aurora-A in carcinomas suggest that inhibitors of these kinases may have inherent potential as therapeutic agents. The structures were determined from crystals grown in nanovolume droplets, which produced high-resolution diffraction data at 1.7, 1.9, and 2.3 A for FAK, Aurora-A, and EphA2, respectively. The FAK and Aurora-A structures are the first determined within two unique subfamilies of human kinases, and all three structures provide new insights into kinase regulation and the design of selective inhibitors.
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