1MP8

Crystal structure of Focal Adhesion Kinase (FAK)

Summary for 1MP8

• Entry DOI: 10.2210/pdb1mp8/pdb
• Related: 1MQ4 1MQB
• Descriptor: focal adhesion kinase 1, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: tyrosine protein kinase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, focal adhesion: Q05397
• Total number of polymer chains: 1
• Total formula weight: 32547.34

Authors

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. (deposition date: 2002-09-11, release date: 2003-09-16, Last modification date: 2024-11-06)

Primary citation

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.
Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography
Structure, 10:1659-1667, 2002

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.

PubMed: 12467573
DOI: 10.1016/S0969-2126(02)00907-3

Experimental method

X-RAY DIFFRACTION (1.6 Å)