The current outbreak of the highly infectious COVID-19 respiratory disease is caused by the novel coronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2). To fight the pandemic, the search for promising viral drug targets has become a cross-border common goal of the international biomedical research community. Within the international Covid19-NMR consortium, scientists support drug development against SARS-CoV-2 by providing publicly available NMR data on viral proteins and RNAs. The coronavirus nucleocapsid protein (N protein) is an RNA-binding protein involved in viral transcription and replication. Its primary function is the packaging of the viral RNA genome. The highly conserved architecture of the coronavirus N protein consists of an N-terminal RNA-binding domain (NTD), followed by an intrinsically disordered Serine/Arginine (SR)-rich linker and a C-terminal dimerization domain (CTD). Besides its involvement in oligomerization, the CTD of the N protein (N-CTD) is also able to bind to nucleic acids by itself, independent of the NTD. Here, we report the near-complete NMR backbone chemical shift assignments of the SARS-CoV-2 N-CTD to provide the basis for downstream applications, in particular site-resolved drug binding studies.
【저자키워드】 SARS-CoV-2, nucleocapsid, structural protein, Solution NMR-spectroscopy, COVID19-NMR, Dimerization domain, Protein druggability, 【초록키워드】 COVID-19, coronavirus, pandemic, Transcription, coronavirus 2, RNAs, nucleocapsid protein, Replication, Protein, nucleic acid, outbreak, International, Respiratory disease, N protein, Community, drug target, NTD, respiratory, oligomerization, NMR, binding, Biomedical research, Support, Viral protein, novel coronavirus SARS-CoV-2, domain, viral RNA genome, backbone, downstream, independent, linker, caused, conserved, involved, in viral, C-terminal, the N protein, intrinsically, CTD, N-terminal RNA-binding domain, the SARS-CoV-2, 【제목키워드】 Protein, domain, backbone, SARS-CoV-2 nucleocapsid, C-terminal,