| Literature DB >> 12467573 |
Jacek Nowakowski1, Ciarán N Cronin, Duncan E McRee, Mark W Knuth, Christian G Nelson, Nikola P Pavletich, Joe Rogers, Bi-Ching Sang, Daniel N Scheibe, Ronald V Swanson, Devon A Thompson.
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.Entities:
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Year: 2002 PMID： 12467573 DOI： 10.1016/s0969-2126(02)00907-3
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006