PDB 1MP8 deposited: 2002-09-11 modified: 2009-02-24
Title Crystal structure of Focal Adhesion Kinase (FAK)
Authors Cronin, C.N., Knuth, M.W., McRee, D.E., Nelson, C.G., Nowakowski, J., Pavletich, N.P., Rodgers, J., Sang, B.-C., Scheibe, D.N., Swanson, R.V., Thompson, D.A.
Structure factors resolution 1.6 rfactor 0.17922 rfree 0.23025
DPI 0.27 theoretical min: 0.11
Related PDB Entries 1MQ4 1MQB

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.

Structure 2002 Dec; 10(12):1659-1667 doi:10.1016/S0969-2126(02)00907-3

Cross References
Database source Identifier Description
PubMed 12467573 STRUE6
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1MP8/0 1MP8 0 monomer 0 1 1 2065