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10.1126/science.abb7498 http://scihub22266oqcxt.onion/10.1126/science.abb7498 32277040!7164392!32277040     free     free     free 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       Science 2020 ; 368 (6492): 779-782 Nephropedia Template TP {{tp|p=32277040|t=2020. Structure of the RNA-dependent RNA polymerase from COVID-19 virus |pdf=|usr=}}{{32277040}} gab.com Text Structure of the RNA-dependent RNA polymerase from COVID-19 virus JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32277040 #FOAvip A novel coronavirus [severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)] outbreak has caused a global coronavirus disease 2019 (COVID-19) pandemic, resulting in tens of thousands of infections and thousands of deaths worldwide. The RNA-dependent RNA polymerase [(RdRp), also named nsp12] is the central component of coronaviral replication and transcription machinery, and it appears to be a primary target for the antiviral drug remdesivir. We report the cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9-angstrom resolution. In addition to the conserved architecture of the polymerase core of the viral polymerase family, nsp12 possesses a newly identified beta-hairpin domain at its N terminus. A comparative analysis model shows how remdesivir binds to this polymerase. The structure provides a basis for the design of new antiviral therapeutics that target viral RdRp. Twit Text FOAVip Structure of the RNA-dependent RNA polymerase from COVID-19 virus ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32277040 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32277040 #FOAvip English Wikipedia <ref>{{Cite pmid|32277040}}</ref> Structure of the RNA-dependent RNA polymerase from COVID-19 virus #MMPMID32277040 Gao Y; Yan L; Huang Y; Liu F; Zhao Y; Cao L; Wang T; Sun Q; Ming Z; Zhang L; Ge J; Zheng L; Zhang Y; Wang H; Zhu Y; Zhu C; Hu T; Hua T; Zhang B; Yang X; Li J; Yang H; Liu Z; Xu W; Guddat LW; Wang Q; Lou Z; Rao Z Science 2020[May]; 368 (6492): 779-782 PMID32277040show ga A novel coronavirus [severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)] outbreak has caused a global coronavirus disease 2019 (COVID-19) pandemic, resulting in tens of thousands of infections and thousands of deaths worldwide. The RNA-dependent RNA polymerase [(RdRp), also named nsp12] is the central component of coronaviral replication and transcription machinery, and it appears to be a primary target for the antiviral drug remdesivir. We report the cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9-angstrom resolution. In addition to the conserved architecture of the polymerase core of the viral polymerase family, nsp12 possesses a newly identified beta-hairpin domain at its N terminus. A comparative analysis model shows how remdesivir binds to this polymerase. The structure provides a basis for the design of new antiviral therapeutics that target viral RdRp. |Adenosine Monophosphate/analogs & derivatives/metabolism/pharmacology[MESH] |Alanine/analogs & derivatives/metabolism/pharmacology[MESH] |Antiviral Agents/metabolism/pharmacology[MESH] |Betacoronavirus/*enzymology[MESH] |Catalytic Domain[MESH] |Coronavirus RNA-Dependent RNA Polymerase[MESH] |Cryoelectron Microscopy[MESH] |Drug Design[MESH] |Models, Molecular[MESH] |Multiprotein Complexes/chemistry/metabolism/ultrastructure[MESH] |Protein Conformation, beta-Strand[MESH] |Protein Domains[MESH] |RNA-Dependent RNA Polymerase/antagonists & inhibitors/*chemistry/metabolism/*ultrastructure[MESH] |SARS-CoV-2[MESH]Structure of the RNA-dependent RNA polymerase from COVID-19 virus (epmc).pdf DeepDyve Pubget Overpricing