1MQB

Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase

Summary for 1MQB

• Entry DOI: 10.2210/pdb1mqb/pdb
• Related: 1MP8 1MQ4
• Descriptor: Ephrin type-A receptor 2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• Functional Keywords: tyrosine protein kinase, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P29317
• Total number of polymer chains: 2
• Total formula weight: 76579.21

Authors

Nowakowski, J.,Cronin, C.N.,McRee, D.E.,Knuth, M.W.,Nelson, C.,Pavletich, N.,Rogers, J.,Sang, B.C.,Scheibe, D.N.,Swanson, R.V.,Thompson, D.A. (deposition date: 2002-09-16, release date: 2003-09-16, Last modification date: 2024-02-14)

Primary citation

Nowakowski, J.,Cronin, C.N.,McRee, D.E.,Knuth, M.W.,Nelson, C.,Pavletich, N.,Rogers, 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, 2003

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 (2.3 Å)