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• W1976096319 abstract "Eukaryotic protein kinases (EPKs) regulate numerous signaling processes by phosphorylating targeted substrates through the highly conserved catalytic domain. Our previous computational studies proposed a model stating that a properly assembled nonlinear motif termed the Regulatory (R) spine is essential for catalytic activity of EPKs. Here we define the required intramolecular interactions and biochemical properties of the R-spine and the newly identified “Shell” that surrounds the R-spine using site-directed mutagenesis and various in vitro phosphoryl transfer assays using cyclic AMP-dependent protein kinase as a representative of the entire kinome. Analysis of the 172 available Apo EPK structures in the protein data bank (PDB) revealed four unique structural conformations of the R-spine that correspond with catalytic inactivation of various EPKs. Elucidating the molecular entities required for the catalytic activation of EPKs and the identification of these inactive conformations opens new avenues for the design of efficient therapeutic EPK inhibitors." @default.
• W1976096319 created "2016-06-24" @default.
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• W1976096319 date "2013-10-15" @default.
• W1976096319 modified "2023-10-17" @default.
• W1976096319 title "Deciphering the Structural Basis of Eukaryotic Protein Kinase Regulation" @default.
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• W1976096319 doi "https://doi.org/10.1371/journal.pbio.1001680" @default.
• W1976096319 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3797032" @default.
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