期刊
MOLECULAR BIOMEDICINE
卷 1, 期 1, 页码 -出版社
SPRINGERNATURE
DOI: 10.1186/s43556-020-00005-0
关键词
SARS-CoV-2; COVID-19; nsp9; Tetramer
资金
- National Key Research and Development Program of China [2017YFA0505903, 2018YFC1312300]
- research fund on COVID-19 of Sichuan Province [2020YFS0010]
- project on COVID-19 of West China Hospital, Sichuan University [HX-2019-nCoV-044]
Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of a potentially fatal disease named coronavirus disease 2019 (COVID-19), has raised significant public health concerns globally. To date, the COVID-19 pandemic has caused millions of people to be infected with SARS-CoV-2 worldwide. It has been known since the 2003 SARS epidemic that coronaviruses (CoVs) have large RNA genomes, the replication of which requires an RNA-dependent RNA replication/transcription complex. CoV nonstructural proteins (Nsps) play pivotal roles in the assembly of this complex and associated enzymatic functions in virus genomic replication. Several smaller nonenzymatic Nsps assist with RNA-dependent RNA polymerase function. In this study, we determined the structure of SARS-CoV-2 nonstructural protein 9 (nsp9), an RNA-binding protein that is essential for CoV replication. Its homotetrameric structure with two stable dimeric interfaces provids a structural basis for understanding the mechanisms of RNA-binding protein self-assembly, which may be essential for the regulation of viral RNA replication and transcription.
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