1H, 13C, and 15N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein

  • 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.

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Author:Sophie KornORCiDGND, Roderick Lambertz, Boris FürtigORCiDGND, Martin HengesbachORCiDGND, Frank LöhrORCiD, Christian RichterORCiDGND, Harald SchwalbeORCiDGND, Julia WeigandORCiDGND, Jens WöhnertORCiDGND, Andreas SchlundtORCiDGND
Parent Title (English):Biomolecular NMR assignments
Place of publication:Dordrecht [u.a.]
Document Type:Article
Date of Publication (online):2020/12/03
Date of first Publication:2020/12/03
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2023/11/23
Tag:Covid19-NMR; Dimerization domain; Nucleocapsid; Protein druggability; SARS-CoV-2; Solution NMR-spectroscopy; Structural protein
Page Number:7
First Page:129
Last Page:135
The Frankfurt BMRZ (Center for Biomolecular Resonance) is supported by the Federal state of Hesse. This work was funded by the Deutsche Forschungsgemeinschaft through grant numbers SFB902/B18 (to Covid19-NMR), SCHL2062/2-1 (to A.S.), the Goethe University Corona funds and by the Johanna Quandt Young Academy at Goethe (grant number 2019/AS01 to A.S.).
Open Access funding enabled and organized by Projekt DEAL.
Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ)
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International