- 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.
MetadatenVerfasserangaben: | Sophie KornORCiDGND, Roderick Lambertz, Boris FürtigORCiDGND, Martin HengesbachORCiDGND, Frank LöhrORCiD, Christian RichterORCiDGND, Harald SchwalbeORCiDGND, Julia WeigandORCiDGND, Jens WöhnertORCiDGND, Andreas SchlundtORCiDGND |
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URN: | urn:nbn:de:hebis:30:3-757137 |
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DOI: | https://doi.org/10.1007/s12104-020-09995-y |
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ISSN: | 1874-270X |
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Titel des übergeordneten Werkes (Englisch): | Biomolecular NMR assignments |
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Verlag: | Springer |
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Verlagsort: | Dordrecht [u.a.] |
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Dokumentart: | Wissenschaftlicher Artikel |
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Sprache: | Englisch |
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Datum der Veröffentlichung (online): | 03.12.2020 |
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Datum der Erstveröffentlichung: | 03.12.2020 |
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Veröffentlichende Institution: | Universitätsbibliothek Johann Christian Senckenberg |
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Datum der Freischaltung: | 23.11.2023 |
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Freies Schlagwort / Tag: | Covid19-NMR; Dimerization domain; Nucleocapsid; Protein druggability; SARS-CoV-2; Solution NMR-spectroscopy; Structural protein |
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Jahrgang: | 15 |
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Ausgabe / Heft: | 1 |
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Seitenzahl: | 7 |
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Erste Seite: | 129 |
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Letzte Seite: | 135 |
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Bemerkung: | 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. |
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HeBIS-PPN: | 516370561 |
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Institute: | Biowissenschaften |
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| Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ) |
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DDC-Klassifikation: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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Sammlungen: | Universitätspublikationen |
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Lizenz (Deutsch): | Creative Commons - CC BY - Namensnennung 4.0 International |
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