Structural highlights
Publication Abstract from PubMedSevere 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. Structural basis for the multimerization of nonstructural protein nsp9 from SARS-CoV-2.,Zhang C, Chen Y, Li L, Yang Y, He J, Chen C, Su D Mol Biomed. 2020 Aug 20;1(1):5. doi: 10.1186/s43556-020-00005-0. PMID:35006420[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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