1mqb
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(New page: 200px<br /> <applet load="1mqb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqb, resolution 2.30Å" /> '''Crystal Structure o...)
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Revision as of 16:07, 12 November 2007
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Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase
Overview
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.
About this Structure
1MQB is a Single protein structure of sequence from Homo sapiens with ANP as ligand. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography., Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA, Structure. 2002 Dec;10(12):1659-67. PMID:12467573
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