Sequence : Nsp8

Total row(s): 2
Select item(s)
Key Findings
Original Article
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Mutation analysis of 2492 SARS-CoV-2 genomes (belonging to 58 different countries representing six continents and five different climatic zones) revealed 1516 nucleotide variations, 744 amino acid substitutions, and 12 deletion sites. The pattern of mutations was different among the six different continents (Europe, Asia, North America, South America, Africa, and Australia) and five different climatic zones (temperate, tropical, diverse, dry, and continental). 32814791
(Sci Rep)
PMID
32814791
Date of Publishing: 2020 Aug 19
Title Genome-wide analysis of SARS-CoV-2 virus strains circulating worldwide implicates heterogeneity
Author(s) nameIslam MR, Hoque MN et al.
Journal Sci Rep
Impact factor
4.12
Citation count: 17
Virus mutagenic capability depends upon several factors, including the fdelity of viral enzymes that replicate nucleic acids, as SARS-CoV-2 RNA dependent RNA polymerase (RdRp) 32321524
(J Transl Med)
PMID
32321524
Date of Publishing: 2020 Apr 22
Title Emerging SARS-CoV-2 mutation hot spots include a novel RNA-dependent-RNA polymerase variant
Author(s) namePachetti M, Marini B et al.
Journal J Transl Med
Impact factor
4.2
Citation count: 119
Date of Entry 2021 Jul 13

Structure : Nsp8

Total row(s): 7
Select item(s)
Key Findings
Original Article
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Structural characterisation of SARS-CoV-2 mini replication and transcription complex 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
Structural characterisation of SARS-CoV-2 mini replication and transcription complex 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 structure of the SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) complex in its active form comprises the non-structural protein 12 (nsp12), nsp8, and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged 'sliding poles'. These sliding poles help in the processivity of RdRp, required for replicating the long genome of coronaviruses. 32438371
(Nature)
PMID
32438371
Date of Publishing: 2020 Aug
Title Structure of replicating SARS-CoV-2 polymerase
Author(s) nameHillen HS, Kokic G et al.
Journal Nature
Impact factor
24.36
Citation count: 74
Structural characterization of cryo-EM structure of the apo nsp12-nsp7-nsp8 complex 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
Structural characteirzation of the nsp12-nsp7-nsp8 complex bound to the template-primer RNA and triphosphate form of Remdesivir(RTP) 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
Structure of SARS-Cov-2 RNA-dependent RNA polymerase nsp12, in complex with nsp7 and nsp8 reports a conserved polymerase core and a β hairpin domain (residues N215 to N218) at its N-terminus. This structure aids in the study of remdesivir and other drug candidates' antiviral activity. 32277040
(Science)
PMID
32277040
Date of Publishing: 2020 May 15
Title Structure of the RNA-dependent RNA polymerase from COVID-19 virus
Author(s) nameGao Y, Yan L et al.
Journal Science
Impact factor
20.57
Citation count: 198
Date of Entry 2021 Jul 28
Structure of SARS-CoV-2 RNA-dependent RNA polymerase nsp12 in complex with cofactors nsp7 and nsp8 under reducing condition, forms a β hairpin domain (residues N215 to N218) at its N-terminus. This structure aids in antiviral viral study of remdesivir and other antiviral drugs. 32277040
(Science)
PMID
32277040
Date of Publishing: 2020 May 15
Title Structure of the RNA-dependent RNA polymerase from COVID-19 virus
Author(s) nameGao Y, Yan L et al.
Journal Science
Impact factor
20.57
Citation count: 198
Date of Entry 2021 Jul 28

Molecular_interactions : Nsp8

Total row(s): 3
Select item(s)
Key Findings
Original Article
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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. 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
Cryo-electron microscopy structure of the SARS-CoV-2 RdRp with non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex, shows active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity and two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Nsp8 along the exiting RNA, forms positively charged 'sliding poles' which affect the processivity of RdRp. 32438371
(Nature)
PMID
32438371
Date of Publishing: 2020 Aug
Title Structure of replicating SARS-CoV-2 polymerase
Author(s) nameHillen HS, Kokic G et al.
Journal Nature
Impact factor
24.36
Citation count: 74
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. 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