Nsp12 is a non-structural protein in the Coronavirus genome. Its gene is part of the ORF1ab reading frame and it is part of the pp1ab polyprotein; it is cleaved by 3CLpro.[1]
Nsp12 is a multi-domain subunit: it consists of an N-terminal nidovirus-specific extension (NiRAN) domain, an interface domain, and a C-terminal RNA-dependent RNA-polymerase domain. The N-terminal portion of SARS-CoV-2 nsp12 additionally contains a β-hairpin which is sandwiched between the NiRAN and RdRp domain.[2]
Coronavirus nsp12 also plays a role in host immune evasion; research has demonstrated that nsp12 inhibits the nuclear translocation of IRF3.[3]
^Snijder, E.J.; Decroly, E.; Ziebuhr, J. (2016), "The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing", Advances in Virus Research, 96, Elsevier: 59–126, doi:10.1016/bs.aivir.2016.08.008, ISBN 978-0-12-804736-1, PMC 7112286, PMID 27712628
^Jiang, Yi; Yin, Wanchao; Xu, H. Eric (2021-01-29). "RNA-dependent RNA polymerase: Structure, mechanism, and drug discovery for COVID-19". Biochemical and Biophysical Research Communications. 538: 47–53. doi:10.1016/j.bbrc.2020.08.116. ISSN 0006-291X. PMC 7473028. PMID 32943188.
Nsp12 is a non-structural protein in the Coronavirus genome. Its gene is part of the ORF1ab reading frame and it is part of the pp1ab polyprotein; it...
nonstructural proteins nsp1-11 and the pp1ab protein contains nsp1-10 and nsp12-16. Proteolytic processing is performed by two proteases: the papain-like...
include various replication proteins such as RNA-dependent RNA polymerase (nsp12), RNA helicase (nsp13), and exoribonuclease (nsp14). A number of the nonstructural...