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10.3390/ijms23010300

http://scihub22266oqcxt.onion/10.3390/ijms23010300
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suck abstract from ncbi


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pmid35008724      Int+J+Mol+Sci 2021 ; 23 (1): ä
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  • Exploring the Catalytic Mechanism of the RNA Cap Modification by nsp16-nsp10 Complex of SARS-CoV-2 through a QM/MM Approach #MMPMID35008724
  • Silva JRA; Urban J; Araujo E; Lameira J; Moliner V; Alves CN
  • Int J Mol Sci 2021[Dec]; 23 (1): ä PMID35008724show ga
  • The inhibition of key enzymes that may contain the viral replication of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have assumed central importance in drug discovery projects. Nonstructural proteins (nsps) are essential for RNA capping and coronavirus replication since it protects the virus from host innate immune restriction. In particular, nonstructural protein 16 (nsp16) in complex with nsp10 is a Cap-0 binding enzyme. The heterodimer formed by nsp16-nsp10 methylates the 5'-end of virally encoded mRNAs to mimic cellular mRNAs and thus it is one of the enzymes that is a potential target for antiviral therapy. In this study, we have evaluated the mechanism of the 2'-O methylation of the viral mRNA cap using hybrid quantum mechanics/molecular mechanics (QM/MM) approach. It was found that the calculated free energy barriers obtained at M062X/6-31+G(d,p) is in agreement with experimental observations. Overall, we provide a detailed molecular analysis of the catalytic mechanism involving the 2'-O methylation of the viral mRNA cap and, as expected, the results demonstrate that the TS stabilization is critical for the catalysis.
  • |Biocatalysis[MESH]
  • |Biomechanical Phenomena[MESH]
  • |Methylation[MESH]
  • |Methyltransferases/chemistry/*metabolism[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Quantum Theory[MESH]
  • |RNA Caps/*chemistry/*metabolism[MESH]
  • |RNA Processing, Post-Transcriptional[MESH]
  • |SARS-CoV-2/*enzymology/*genetics[MESH]
  • |Viral Nonstructural Proteins/chemistry/*metabolism[MESH]


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