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• W2109816304 abstract "The c-Src tyrosine kinase co-operates with the focal adhesion kinase to regulate cell adhesion and motility. Focal adhesion kinase engages the regulatory SH3 and SH2 domains of c-Src, resulting in localized kinase activation that contributes to tumor cell metastasis. Using assay conditions where c-Src kinase activity required binding to a tyrosine phosphopeptide based on the focal adhesion kinase SH3-SH2 docking sequence, we screened a kinase-biased library for selective inhibitors of the Src/focal adhesion kinase peptide complex versus c-Src alone. This approach identified an aminopyrimidinyl carbamate compound, WH-4-124-2, with nanomolar inhibitory potency and fivefold selectivity for c-Src when bound to the phospho-focal adhesion kinase peptide. Molecular docking studies indicate that WH-4-124-2 may preferentially inhibit the ‘DFG-out’ conformation of the kinase active site. These findings suggest that interaction of c-Src with focal adhesion kinase induces a unique kinase domain conformation amenable to selective inhibition." @default.
• W2109816304 created "2016-06-24" @default.
• W2109816304 creator A5021415113 @default.
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• W2109816304 date "2014-11-28" @default.
• W2109816304 modified "2023-10-17" @default.
• W2109816304 title "A Discovery Strategy for Selective Inhibitors of c-Src in Complex with the Focal Adhesion Kinase SH3/SH2-binding Region" @default.
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• W2109816304 doi "https://doi.org/10.1111/cbdd.12473" @default.
• W2109816304 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4444405" @default.
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