Korn, Sophie M. ; Dhamotharan, Karthikeyan ; Fürtig, Boris ; Hengesbach, Martin ; Löhr, Frank ; Qureshi, Nusrat S. ; Richter, Christian ; Saxena, Krishna ; Schwalbe, Harald ; Tants, Jan-Niklas ; Weigand, Julia E. ; Wöhnert, Jens ; Schlundt, Andreas (2020)
¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e.
In: Biomolecular NMR Assignments, 14 (2)
doi: 10.1007/s12104-020-09971-6
Artikel, Bibliographie
Dies ist die neueste Version dieses Eintrags.
Kurzbeschreibung (Abstract)
The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus’ proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2020 |
| Autor(en): | Korn, Sophie M. ; Dhamotharan, Karthikeyan ; Fürtig, Boris ; Hengesbach, Martin ; Löhr, Frank ; Qureshi, Nusrat S. ; Richter, Christian ; Saxena, Krishna ; Schwalbe, Harald ; Tants, Jan-Niklas ; Weigand, Julia E. ; Wöhnert, Jens ; Schlundt, Andreas |
| Art des Eintrags: | Bibliographie |
| Titel: | ¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e |
| Sprache: | Englisch |
| Publikationsjahr: | Oktober 2020 |
| Ort: | Dordrecht |
| Verlag: | Springer Netherlands |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Biomolecular NMR Assignments |
| Jahrgang/Volume einer Zeitschrift: | 14 |
| (Heft-)Nummer: | 2 |
| DOI: | 10.1007/s12104-020-09971-6 |
| Zugehörige Links: | |
| Kurzbeschreibung (Abstract): | The ongoing pandemic caused by the Betacoronavirus SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus-2) demonstrates the urgent need of coordinated and rapid research towards inhibitors of the COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome encodes for approximately 30 proteins, among them are the 16 so-called non-structural proteins (Nsps) of the replication/transcription complex. The 217-kDa large Nsp3 spans one polypeptide chain, but comprises multiple independent, yet functionally related domains including the viral papain-like protease. The Nsp3e sub-moiety contains a putative nucleic acid-binding domain (NAB) with so far unknown function and consensus target sequences, which are conceived to be both viral and host RNAs and DNAs, as well as protein-protein interactions. Its NMR-suitable size renders it an attractive object to study, both for understanding the SARS-CoV-2 architecture and drugability besides the classical virus’ proteases. We here report the near-complete NMR backbone chemical shifts of the putative Nsp3e NAB that reveal the secondary structure and compactness of the domain, and provide a basis for NMR-based investigations towards understanding and interfering with RNA- and small-molecule-binding by Nsp3e. |
| Freie Schlagworte: | SARS-CoV-2, Non-structural protein, Nucleic acid-binding domain, Solution NMR-spectroscopy, Protein drugability, Covid19-NMR |
| 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: | 19 Dez 2024 09:34 |
| Letzte Änderung: | 19 Dez 2024 12:33 |
| PPN: | 524853452 |
| Export: | |
| Suche nach Titel in: | TUfind oder in Google |
Verfügbare Versionen dieses Eintrags
-
¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e. (deposited 18 Dez 2024 12:57)
- ¹H, ¹³C, and ¹⁵N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e. (deposited 19 Dez 2024 09:34) [Gegenwärtig angezeigt]
 |
Frage zum Eintrag |
Optionen (nur für Redakteure)
 |
Redaktionelle Details anzeigen |
Drucken
Impressum