Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography.

Article Details

Citation

Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA

Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography.

Structure. 2002 Dec;10(12):1659-67.

PubMed ID
12467573 [ View in 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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Ephrin type-A receptor 2P29317Details
Aurora kinase AO14965Details
Focal adhesion kinase 1Q05397Details