Viral protein-nucleic acid


Last updated: 2021 Jul 28
Total hit(s): 3
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Original Article
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Host protein arginine methyltransferases (PRMTs) methylates SARS-CoV-2 N protein at residues R95 and R177 within RGG/RG motifs.Type I PRMT inhibitor (MS023) or substitution of R95 or R177 with lysine inhibits interaction of N protein with the 5-UTR of SARS-CoV-2 genomic RNA, a property required for viral packaging. Type I PRMT inhibitors (MS023), cancer drug canditates, have found to reduce SARS-CoV-2 production by inhibiting the methylation of arginine in the N protein of SARS-CoV-2 and hence are promising antivirals.
34029587
(J Biol Chem)
PMID
34029587
Date of Publishing: 2021 May 23
Title Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication
Author(s) nameCai T, Yu Z et al.
Journal J Biol Chem
Impact factor
3.96
Citation count: 1
Date of Entry 2021 Jul 28


Nsp13-1 stabilizes SARS-CoV-2 replication and transcription (RTC) complex by contacting with nsp13-2, which anchors the 5'-extension of RNA template, and interacting with nsp7-nsp8-nsp12-RNA. Different orientations of nsp13-1 results in different interactions with the two forms of mini RTC. Mini RTC with an nsp12R365A mutation has greater helicase activity compared to individual apsnsp13. Nsp13-1T216A mutation has a decreased helicase activity.
33208736
(Nat Commun)
PMID
33208736
Date of Publishing: 2020 Nov 18
Title Architecture of a SARS-CoV-2 mini replication and transcription complex
Author(s) nameYan L, Zhang Y et al.
Journal Nat Commun
Impact factor
11.8
Citation count: 4


The complex cryo-electron microscopy structure of SARS-CoV-2 RdRp with a 50-base template-primer RNA and remdesivir, shows the partial double-stranded RNA template is present in the central channel of RdRp where remdesivir is covalently attached as the first replicated base pair and results in the termination of chain elongation. The conserved protein-RNA interactions and the catalytic active site residues, in the diverse RNA viruses, makes it possible to develop broad spectrum antiviral inhibitors.
32358203
(Science)
PMID
32358203
Date of Publishing: 2020 Jun 26
Title Structural basis for inhibition of the RNA-dependent RNA polymerase from SARS-CoV-2 by remdesivir
Author(s) nameYin W, Mao C et al.
Journal Science
Impact factor
20.57
Citation count: 156