Download MendeleyStructures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography
Nowakowski, J., Cronin, C.N., McRee, D.E., Knuth, M.W., Nelson, C.G., Pavletich, N.P., Rodgers, J., Sang, B.-C., Scheibe, D.N., Swanson, R.V., Thompson, D.A.(2002) 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.
Organizational Affiliation:
Syrrx, Inc., 10410 Science Center Drive, San Diego, CA 92121, USA. [email protected]
