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10.1073/pnas.2021946118 http://scihub22266oqcxt.onion/10.1073/pnas.2021946118 33526596!7896311!33526596     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (7): ä Nephropedia Template TP {{tp|p=33526596|t=2021. Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP |pdf=|usr=}}{{33526596}} gab.com Text Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33526596 #FOAvip The RNA polymerase inhibitor favipiravir is currently in clinical trials as a treatment for infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), despite limited information about the molecular basis for its activity. Here we report the structure of favipiravir ribonucleoside triphosphate (favipiravir-RTP) in complex with the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) bound to a template:primer RNA duplex, determined by electron cryomicroscopy (cryoEM) to a resolution of 2.5 A. The structure shows clear evidence for the inhibitor at the catalytic site of the enzyme, and resolves the conformation of key side chains and ions surrounding the binding pocket. Polymerase activity assays indicate that the inhibitor is weakly incorporated into the RNA primer strand, and suppresses RNA replication in the presence of natural nucleotides. The structure reveals an unusual, nonproductive binding mode of favipiravir-RTP at the catalytic site of SARS-CoV-2 RdRp, which explains its low rate of incorporation into the RNA primer strand. Together, these findings inform current and future efforts to develop polymerase inhibitors for SARS coronaviruses. Twit Text FOAVip Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33526596 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33526596 #FOAvip English Wikipedia <ref>{{Cite pmid|33526596}}</ref> Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP #MMPMID33526596 Naydenova K; Muir KW; Wu LF; Zhang Z; Coscia F; Peet MJ; Castro-Hartmann P; Qian P; Sader K; Dent K; Kimanius D; Sutherland JD; Lowe J; Barford D; Russo CJ Proc Natl Acad Sci U S A 2021[Feb]; 118 (7): ä PMID33526596show ga The RNA polymerase inhibitor favipiravir is currently in clinical trials as a treatment for infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), despite limited information about the molecular basis for its activity. Here we report the structure of favipiravir ribonucleoside triphosphate (favipiravir-RTP) in complex with the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) bound to a template:primer RNA duplex, determined by electron cryomicroscopy (cryoEM) to a resolution of 2.5 A. The structure shows clear evidence for the inhibitor at the catalytic site of the enzyme, and resolves the conformation of key side chains and ions surrounding the binding pocket. Polymerase activity assays indicate that the inhibitor is weakly incorporated into the RNA primer strand, and suppresses RNA replication in the presence of natural nucleotides. The structure reveals an unusual, nonproductive binding mode of favipiravir-RTP at the catalytic site of SARS-CoV-2 RdRp, which explains its low rate of incorporation into the RNA primer strand. Together, these findings inform current and future efforts to develop polymerase inhibitors for SARS coronaviruses. |Amides/chemistry/*pharmacology[MESH] |Coronavirus RNA-Dependent RNA Polymerase/antagonists & inhibitors/chemistry/*metabolism[MESH] |Cryoelectron Microscopy/methods[MESH] |Enzyme Inhibitors/chemistry/*pharmacology[MESH] |Pyrazines/chemistry/*pharmacology[MESH] |Ribonucleotides/chemistry[MESH] |SARS-CoV-2/drug effects/enzymology/*ultrastructure[MESH]Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presen(epmc).pdf DeepDyve Pubget Overpricing