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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 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28712745 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28712745 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       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? 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 PMID28712745 show 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? 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. |*Ligands [MESH] |Adenosine Triphosphate/chemistry/metabolism [MESH] |Binding Sites [MESH] |Chromatography, High Pressure Liquid [MESH] |Diacylglycerol Kinase/chemistry/genetics/*metabolism [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Isotope Labeling [MESH] |Ketanserin/chemistry/metabolism [MESH] |Peptides/analysis [MESH] |Protein Binding [MESH] |Protein Isoforms/chemistry/genetics/metabolism [MESH] |Proteome/analysis [MESH] |Recombinant Proteins/biosynthesis/chemistry/isolation & purification [MESH] |Ritanserin/chemistry/metabolism [MESH]The Ligand Binding Landscape of Diacylglycerol Kinases (epmc).pdf DeepDyve Pubget Overpricing