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10.1021/acs.jmedchem.1c00063 http://scihub22266oqcxt.onion/10.1021/acs.jmedchem.1c00063 34323071!ä!34323071 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Med+Chem 2022 ; 65 (2): 1302-1312 Nephropedia Template TP {{tp|p=34323071|t=2022. Molecular Plasticity of Crystalline CK2alpha Leads to KN2, a Bivalent Inhibitor of Protein Kinase CK2 with Extraordinary Selectivity |pdf=|usr=}}{{34323071}} gab.com Text Molecular Plasticity of Crystalline CK2alpha Leads to KN2, a Bivalent Inhibitor of Protein Kinase CK2 with Extraordinary Selectivity JO: J Med Chem http://www.kidney.de/pget.php?&tw=1&pmid=34323071 #FOAvip CK2alpha and CK2alpha' are paralogous catalytic subunits of CK2, which belongs to the eukaryotic protein kinases. CK2 promotes tumorigenesis and the spread of pathogenic viruses like SARS-CoV-2 and is thus an attractive drug target. Efforts to develop selective CK2 inhibitors binding offside the ATP site had disclosed the alphaD pocket in CK2alpha; its occupation requires large conformational adaptations of the helix alphaD. As shown here, the alphaD pocket is accessible also in CK2alpha', where the necessary structural plasticity can be triggered with suitable ligands even in the crystalline state. A CK2alpha' structure with an ATP site and an alphaD pocket ligand guided the design of the bivalent CK2 inhibitor KN2. It binds to CK2 with low nanomolar affinity, is cell-permeable, and suppresses the intracellular phosphorylation of typical CK2 substrates. Kinase profiling revealed a high selectivity of KN2 for CK2 and emphasizes the selectivity-promoting potential of the alphaD pocket. Twit Text FOAVip Molecular Plasticity of Crystalline CK2alpha Leads to KN2, a Bivalent Inhibitor of Protein Kinase CK2 with Extraordinary Selectivity ????J Med Chem http://www.kidney.de/pget.php?&tw=1&pmid=34323071 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34323071 #FOAvip English Wikipedia <ref>{{Cite pmid|34323071}}</ref> Molecular Plasticity of Crystalline CK2alpha Leads to KN2, a Bivalent Inhibitor of Protein Kinase CK2 with Extraordinary Selectivity #MMPMID34323071 Lindenblatt D; Applegate V; Nickelsen A; Klussmann M; Neundorf I; Gotz C; Jose J; Niefind K J Med Chem 2022[Jan]; 65 (2): 1302-1312 PMID34323071show ga CK2alpha and CK2alpha' are paralogous catalytic subunits of CK2, which belongs to the eukaryotic protein kinases. CK2 promotes tumorigenesis and the spread of pathogenic viruses like SARS-CoV-2 and is thus an attractive drug target. Efforts to develop selective CK2 inhibitors binding offside the ATP site had disclosed the alphaD pocket in CK2alpha; its occupation requires large conformational adaptations of the helix alphaD. As shown here, the alphaD pocket is accessible also in CK2alpha', where the necessary structural plasticity can be triggered with suitable ligands even in the crystalline state. A CK2alpha' structure with an ATP site and an alphaD pocket ligand guided the design of the bivalent CK2 inhibitor KN2. It binds to CK2 with low nanomolar affinity, is cell-permeable, and suppresses the intracellular phosphorylation of typical CK2 substrates. Kinase profiling revealed a high selectivity of KN2 for CK2 and emphasizes the selectivity-promoting potential of the alphaD pocket. |Adenosine Triphosphate/metabolism[MESH] |Casein Kinase II/*antagonists & inhibitors/chemistry/metabolism[MESH] |Crystallization[MESH] |HEK293 Cells[MESH] |HeLa Cells[MESH] |Humans[MESH] |Ligands[MESH] |Phosphorylation[MESH] |Protein Conformation[MESH] |Protein Kinase Inhibitors/*pharmacology[MESH]Molecular Plasticity of Crystalline CK2alpha Leads to KN2, a Bivalent(epmc).pdf DeepDyve Pubget Overpricing