1 H, 13 C, and 15 N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid
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ARTICLE
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H, 13C, and 15N backbone chemical shift assignments of the C‑terminal dimerization domain of SARS‑CoV‑2 nucleocapsid protein Sophie M. Korn1,4 · Roderick Lambertz1 · Boris Fürtig2,4 · Martin Hengesbach2 · Frank Löhr3,4 · Christian Richter2,4 · Harald Schwalbe2,4 · Julia E. Weigand5 · Jens Wöhnert1,4 · Andreas Schlundt1,4 Received: 24 October 2020 / Accepted: 25 November 2020 © The Author(s) 2020
Abstract 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. Keywords SARS-CoV-2 · Structural protein · Nucleocapsid · Dimerization domain · Solution NMR-spectroscopy · Protein druggability · Covid19-NMR
Biological context
* Andreas Schlundt [email protected]‑frankfurt.de; covid19‑[email protected]‑frankfurt.de 1
Institute for Molecular Biosciences, Johann Wolfgang Goethe-University Frankfurt, Max‑von‑Laue‑Str. 9, 60438 Frankfurt/M, Germany
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Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max‑von‑Laue‑Str. 7, 60438 Frankfurt/M, Germany
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Institute of Biophysical Chemistry, Johann Wolfgang Goethe-University Frankfurt, Max‑von‑Laue‑Str. 9, 60438 Frankfurt/M, Germany
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Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University Frankfurt, 60438 Frankfurt/M, Germany
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Department of Biology, Technical University of Darmstadt, Schnittspahnstr. 10, 64287 Darmstadt, Germany
SARS-CoV-2 is the newest representative of the coronavirus family transmissible to humans and the cause of the COVID-19 respiratory disease. SARS-CoV-2, together with the closely related SARS-CoV (~ 79% sequence homology) and the Middle East Respiratory Syndrome (MERS)-CoV (~ 50% sequence homology), belongs to the genus of Betacoronaviridae and is one of seven known human-pathogenic CoVs (Chen et al. 2020). As of late September 2020, th
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