4k9y

FOCAL ADHESION KINASE Catalytic domain in complex with 1-[4-(6-Amino-purin-9-yl)-phenyl]-3-(5-tert-butyl-2-p-tolyl-2H-pyrazol-3-yl)-urea

spinqualitylabelsall models 4k9y, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4k9y is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: K9Y Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Chemically diverse fragment hits of focal adhesion kinase (FAK) were discovered by surface plasmon resonance (SPR) screening of our in-house fragment library. Site specific binding of the primary hits was confirmed in a competition setup using a high-affinity ATP-site inhibitor of FAK. Protein crystallography revealed the binding mode of 41 out of 48 selected fragment hits within the ATP-site. Structural comparison of the fragment binding modes with a DFG-out inhibitor of FAK initiated first synthetic follow-up optimization leading to improved binding affinity. Fragment-based discovery of focal adhesion kinase inhibitors.,Gradler U, Bomke J, Musil D, Dresing V, Lehmann M, Holzemann G, Greiner H, Esdar C, Krier M, Heinrich T Bioorg Med Chem Lett. 2013 Oct 1;23(19):5401-9. doi: 10.1016/j.bmcl.2013.07.050. , Epub 2013 Jul 31. PMID:23973211 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Focal adhesion kinase 3D structures

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