Korn, Sophie M. ; Lambertz, Roderick ; Fürtig, Boris ; Hengesbach, Martin ; Löhr, Frank ; Richter, Christian ; Schwalbe, Harald ; Weigand, Julia E. ; Wöhnert, Jens ; Schlundt, Andreas (2024)
¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein.
In: Biomolecular NMR Assignments, 2021, 15 (1)
doi: 10.26083/tuprints-00023999
Artikel, Zweitveröffentlichung, Verlagsversion
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Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2024 |
| Autor(en): | Korn, Sophie M. ; Lambertz, Roderick ; Fürtig, Boris ; Hengesbach, Martin ; Löhr, Frank ; Richter, Christian ; Schwalbe, Harald ; Weigand, Julia E. ; Wöhnert, Jens ; Schlundt, Andreas |
| Art des Eintrags: | Zweitveröffentlichung |
| Titel: | ¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein |
| Sprache: | Englisch |
| Publikationsjahr: | 18 Dezember 2024 |
| Ort: | Darmstadt |
| Publikationsdatum der Erstveröffentlichung: | April 2021 |
| Ort der Erstveröffentlichung: | Dordrecht |
| Verlag: | Springer Netherlands |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Biomolecular NMR Assignments |
| Jahrgang/Volume einer Zeitschrift: | 15 |
| (Heft-)Nummer: | 1 |
| DOI: | 10.26083/tuprints-00023999 |
| URL / URN: | https://tuprints.ulb.tu-darmstadt.de/23999 |
| Zugehörige Links: | |
| Herkunft: | Zweitveröffentlichung DeepGreen |
| Kurzbeschreibung (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. |
| Freie Schlagworte: | SARS-CoV-2, Structural protein, Nucleocapsid, Dimerization domain, Solution NMR-spectroscopy, Protein druggability, Covid19-NMR |
| Status: | Verlagsversion |
| URN: | urn:nbn:de:tuda-tuprints-239998 |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 540 Chemie 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie 600 Technik, Medizin, angewandte Wissenschaften > 610 Medizin, Gesundheit |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > RNA Biochemie |
| Hinterlegungsdatum: | 18 Dez 2024 12:54 |
| Letzte Änderung: | 19 Dez 2024 09:35 |
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| Suche nach Titel in: | TUfind oder in Google |
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- ¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the C-terminal dimerization domain of SARS-CoV-2 nucleocapsid protein. (deposited 18 Dez 2024 12:54) [Gegenwärtig angezeigt]
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