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10.1038/s41467-020-17496-8 http://scihub22266oqcxt.onion/10.1038/s41467-020-17496-8 32709886!7381649!32709886     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       Nat+Commun 2020 ; 11 (1): 3718 Nephropedia Template TP {{tp|p=32709886|t=2020. Structural basis of RNA cap modification by SARS-CoV-2 |pdf=|usr=}}{{32709886}} gab.com Text Structural basis of RNA cap modification by SARS-CoV-2 JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32709886 #FOAvip The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 illness, has caused millions of infections worldwide. In SARS coronaviruses, the non-structural protein 16 (nsp16), in conjunction with nsp10, methylates the 5'-end of virally encoded mRNAs to mimic cellular mRNAs, thus protecting the virus from host innate immune restriction. We report here the high-resolution structure of a ternary complex of SARS-CoV-2 nsp16 and nsp10 in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine (SAM). The nsp16/nsp10 heterodimer is captured in the act of 2'-O methylation of the ribose sugar of the first nucleotide of SARS-CoV-2 mRNA. We observe large conformational changes associated with substrate binding as the enzyme transitions from a binary to a ternary state. This induced fit model provides mechanistic insights into the 2'-O methylation of the viral mRNA cap. We also discover a distant (25 A) ligand-binding site unique to SARS-CoV-2, which can alternatively be targeted, in addition to RNA cap and SAM pockets, for antiviral development. Twit Text FOAVip Structural basis of RNA cap modification by SARS-CoV-2 ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32709886 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32709886 #FOAvip English Wikipedia <ref>{{Cite pmid|32709886}}</ref> Structural basis of RNA cap modification by SARS-CoV-2 #MMPMID32709886 Viswanathan T; Arya S; Chan SH; Qi S; Dai N; Misra A; Park JG; Oladunni F; Kovalskyy D; Hromas RA; Martinez-Sobrido L; Gupta YK Nat Commun 2020[Jul]; 11 (1): 3718 PMID32709886show ga The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 illness, has caused millions of infections worldwide. In SARS coronaviruses, the non-structural protein 16 (nsp16), in conjunction with nsp10, methylates the 5'-end of virally encoded mRNAs to mimic cellular mRNAs, thus protecting the virus from host innate immune restriction. We report here the high-resolution structure of a ternary complex of SARS-CoV-2 nsp16 and nsp10 in the presence of cognate RNA substrate analogue and methyl donor, S-adenosyl methionine (SAM). The nsp16/nsp10 heterodimer is captured in the act of 2'-O methylation of the ribose sugar of the first nucleotide of SARS-CoV-2 mRNA. We observe large conformational changes associated with substrate binding as the enzyme transitions from a binary to a ternary state. This induced fit model provides mechanistic insights into the 2'-O methylation of the viral mRNA cap. We also discover a distant (25 A) ligand-binding site unique to SARS-CoV-2, which can alternatively be targeted, in addition to RNA cap and SAM pockets, for antiviral development. |Betacoronavirus[MESH] |COVID-19[MESH] |Coronavirus Infections/virology[MESH] |Humans[MESH] |Methyltransferases/*chemistry/metabolism[MESH] |Models, Chemical[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Pneumonia, Viral/virology[MESH] |RNA Caps/*metabolism[MESH] |RNA, Viral/metabolism[MESH] |S-Adenosylmethionine/metabolism[MESH] |SARS-CoV-2[MESH] |Viral Nonstructural Proteins/*chemistry/metabolism[MESH] |Viral Regulatory and Accessory Proteins/*chemistry/metabolism[MESH]Structural basis of RNA cap modification by SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing