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.

当前爆发的高传染性COVID-19呼吸道疾病是由新型冠状病毒SARS-CoV-2（严重急性呼吸综合征冠状病毒2）引起的。为抗击疫情，寻找有前景的病毒药物靶点已成为国际生物医学研究界跨境的共同目标。在国际Covid19-NMR联盟中，科学家们通过提供有关病毒蛋白和 RNA 的公开 NMR 数据来支持针对 SARS-CoV-2 的药物开发。冠状病毒核衣壳蛋白（N蛋白）是一种参与病毒转录和复制的RNA结合蛋白。它的主要功能是包装病毒RNA基因组。冠状病毒 N 蛋白的高度保守结构由 N 端 RNA 结合结构域 (NTD)、随后的本质上无序的富含丝氨酸/精氨酸 (SR) 的接头和 C 端二聚化结构域 (CTD) 组成。除了参与寡聚化之外，N 蛋白的 CTD (N-CTD) 还能够独立于 NTD 自身与核酸结合。在这里，我们报告了 SARS-CoV-2 N-CTD 的近乎完整的 NMR 主链化学位移分配，为下游应用，特别是位点解析药物结合研究提供基础。