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10.1016/j.jbc.2021.101218 http://scihub22266oqcxt.onion/10.1016/j.jbc.2021.101218 34562452!8494237!34562452     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2021 ; 297 (4): 101218 Nephropedia Template TP {{tp|p=34562452|t=2021. An atomistic model of the coronavirus replication-transcription complex as a hexamer assembled around nsp15 |pdf=|usr=}}{{34562452}} gab.com Text An atomistic model of the coronavirus replication-transcription complex as a hexamer assembled around nsp15 JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=34562452 #FOAvip The SARS-CoV-2 replication-transcription complex is an assembly of nonstructural viral proteins that collectively act to reproduce the viral genome and generate mRNA transcripts. While the structures of the individual proteins involved are known, how they assemble into a functioning superstructure is not. Applying molecular modeling tools, including protein-protein docking, to the available structures of nsp7-nsp16 and the nucleocapsid, we have constructed an atomistic model of how these proteins associate. Our principal finding is that the complex is hexameric, centered on nsp15. The nsp15 hexamer is capped on two faces by trimers of nsp14/nsp16/(nsp10)(2), which then recruit six nsp12/nsp7/(nsp8)(2) polymerase subunits to the complex. To this, six subunits of nsp13 are arranged around the superstructure, but not evenly distributed. Polymerase subunits that coordinate dimers of nsp13 are capable of binding the nucleocapsid, which positions the 5'-UTR TRS-L RNA over the polymerase active site, a state distinguishing transcription from replication. Analysis of the viral RNA path through the complex indicates the dsRNA that exits the polymerase passes over the nsp14 exonuclease and nsp15 endonuclease sites before being unwound by a convergence of zinc fingers from nsp10 and nsp14. The template strand is then directed away from the complex, while the nascent strand is directed to the sites responsible for mRNA capping. The model presents a cohesive picture of the multiple functions of the coronavirus replication-transcription complex and addresses fundamental questions related to proofreading, template switching, mRNA capping, and the role of the endonuclease. Twit Text FOAVip An atomistic model of the coronavirus replication-transcription complex as a hexamer assembled around nsp15 ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=34562452 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34562452 #FOAvip English Wikipedia <ref>{{Cite pmid|34562452}}</ref> An atomistic model of the coronavirus replication-transcription complex as a hexamer assembled around nsp15 #MMPMID34562452 Perry JK; Appleby TC; Bilello JP; Feng JY; Schmitz U; Campbell EA J Biol Chem 2021[Oct]; 297 (4): 101218 PMID34562452show ga The SARS-CoV-2 replication-transcription complex is an assembly of nonstructural viral proteins that collectively act to reproduce the viral genome and generate mRNA transcripts. While the structures of the individual proteins involved are known, how they assemble into a functioning superstructure is not. Applying molecular modeling tools, including protein-protein docking, to the available structures of nsp7-nsp16 and the nucleocapsid, we have constructed an atomistic model of how these proteins associate. Our principal finding is that the complex is hexameric, centered on nsp15. The nsp15 hexamer is capped on two faces by trimers of nsp14/nsp16/(nsp10)(2), which then recruit six nsp12/nsp7/(nsp8)(2) polymerase subunits to the complex. To this, six subunits of nsp13 are arranged around the superstructure, but not evenly distributed. Polymerase subunits that coordinate dimers of nsp13 are capable of binding the nucleocapsid, which positions the 5'-UTR TRS-L RNA over the polymerase active site, a state distinguishing transcription from replication. Analysis of the viral RNA path through the complex indicates the dsRNA that exits the polymerase passes over the nsp14 exonuclease and nsp15 endonuclease sites before being unwound by a convergence of zinc fingers from nsp10 and nsp14. The template strand is then directed away from the complex, while the nascent strand is directed to the sites responsible for mRNA capping. The model presents a cohesive picture of the multiple functions of the coronavirus replication-transcription complex and addresses fundamental questions related to proofreading, template switching, mRNA capping, and the role of the endonuclease. |*Models, Molecular[MESH] |Binding Sites[MESH] |COVID-19/pathology/virology[MESH] |Dimerization[MESH] |Endoribonucleases/chemistry/genetics/*metabolism[MESH] |Humans[MESH] |Molecular Docking Simulation[MESH] |Protein Structure, Quaternary[MESH] |RNA, Double-Stranded/chemistry/metabolism[MESH] |SARS-CoV-2/isolation & purification/*metabolism[MESH] |Transcription, Genetic[MESH] |Viral Nonstructural Proteins/chemistry/genetics/*metabolism[MESH]An atomistic model of the coronavirus replication-transcription comple(epmc).pdf DeepDyve Pubget Overpricing