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10.1016/j.chembiol.2017.06.007 http://scihub22266oqcxt.onion/10.1016/j.chembiol.2017.06.007 C5551460!5551460!28712745     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Chem+Biol 2017 ; 24 (7): 870-880.e5 Nephropedia Template TP {{tp|p=28712745|t=2017. The Ligand Binding Landscape of Diacylglycerol Kinases |pdf=|usr=}}{{28712745}} gab.com Text The Ligand Binding Landscape of Diacylglycerol Kinases JO: Cell Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28712745 #FOAvip Diacylglycerol kinases (DGKs) are integral components of signal transduction cascades that regulate cell biology through ATP-dependent phosphorylation of the lipid messenger diacylglycerol. Methods for direct evaluation of DGK activity in native biological systems are lacking and needed to study isoform-specific functions of these multidomain lipid kinases. Here, we utilize ATP acyl phosphate activity-based probes and quantitative mass spectrometry to define, for the first time, ATP- and small molecule-binding motifs of representative members from all five DGK subtypes. We use chemical proteomics to discover an unusual binding mode for the DGK-alpha (DGK?) inhibitor ritanserin, including interactions at the atypical C1 domain distinct from the ATP binding region. Unexpectedly, deconstruction of ritanserin yielded a fragment compound that blocks DGK? activity through a conserved binding mode and enhanced selectivity against the kinome. Collectively, our studies illustrate the power of chemical proteomics to profile protein-small molecule interactions of lipid kinases for fragment-based lead discovery. Twit Text FOAVip The Ligand Binding Landscape of Diacylglycerol Kinases ????Cell Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28712745 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28712745 #FOAvip English Wikipedia <ref>{{Cite pmid|28712745}}</ref> The Ligand Binding Landscape of Diacylglycerol Kinases #MMPMID28712745 Franks CE; Campbell ST; Purow BW; Harris TE; Hsu KL Cell Chem Biol 2017[Jul]; 24 (7): 870-880.e5 PMID28712745show ga Diacylglycerol kinases (DGKs) are integral components of signal transduction cascades that regulate cell biology through ATP-dependent phosphorylation of the lipid messenger diacylglycerol. Methods for direct evaluation of DGK activity in native biological systems are lacking and needed to study isoform-specific functions of these multidomain lipid kinases. Here, we utilize ATP acyl phosphate activity-based probes and quantitative mass spectrometry to define, for the first time, ATP- and small molecule-binding motifs of representative members from all five DGK subtypes. We use chemical proteomics to discover an unusual binding mode for the DGK-alpha (DGK?) inhibitor ritanserin, including interactions at the atypical C1 domain distinct from the ATP binding region. Unexpectedly, deconstruction of ritanserin yielded a fragment compound that blocks DGK? activity through a conserved binding mode and enhanced selectivity against the kinome. Collectively, our studies illustrate the power of chemical proteomics to profile protein-small molecule interactions of lipid kinases for fragment-based lead discovery. äThe Ligand Binding Landscape of Diacylglycerol Kinases (epmc).pdf DeepDyve Pubget Overpricing