Kubatova, N. ; Qureshi, N. S. ; Altincekic, N. ; Abele, R. ; Bains, J. K. ; Ceylan, B. ; Ferner, J. ; Fuks, C. ; Hargittay, B. ; Hutchison, M. T. ; de Jesus, V. ; Kutz, F. ; Wirtz Martin, M. A. ; Meiser, N. ; Linhard, V. ; Pyper, D. J. ; Trucks, S. ; Fürtig, B. ; Hengesbach, M. ; Löhr, F. ; Richter, C. ; Saxena, K. ; Schlundt, A. ; Schwalbe, H. ; Sreeramulu, S. ; Wacker, A. ; Weigand, Julia E. ; Wirmer-Bartoschek, J. ; Wöhnert, J. (2020)
1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10.
In: Biomolecular NMR assignments, 2020
doi: 10.1007/s12104-020-09984-1
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
The international Covid19-NMR consortium aims at the comprehensive spectroscopic characterization of SARS-CoV-2 RNA elements and proteins and will provide NMR chemical shift assignments of the molecular components of this virus. The SARS-CoV-2 genome encodes approximately 30 different proteins. Four of these proteins are involved in forming the viral envelope or in the packaging of the RNA genome and are therefore called structural proteins. The other proteins fulfill a variety of functions during the viral life cycle and comprise the so-called non-structural proteins (nsps). Here, we report the near-complete NMR resonance assignment for the backbone chemical shifts of the non-structural protein 10 (nsp10). Nsp10 is part of the viral replication-transcription complex (RTC). It aids in synthesizing and modifying the genomic and subgenomic RNAs. Via its interaction with nsp14, it ensures transcriptional fidelity of the RNA-dependent RNA polymerase, and through its stimulation of the methyltransferase activity of nsp16, it aids in synthesizing the RNA cap structures which protect the viral RNAs from being recognized by the innate immune system. Both of these functions can be potentially targeted by drugs. Our data will aid in performing additional NMR-based characterizations, and provide a basis for the identification of possible small molecule ligands interfering with nsp10 exerting its essential role in viral replication.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2020 |
| Autor(en): | Kubatova, N. ; Qureshi, N. S. ; Altincekic, N. ; Abele, R. ; Bains, J. K. ; Ceylan, B. ; Ferner, J. ; Fuks, C. ; Hargittay, B. ; Hutchison, M. T. ; de Jesus, V. ; Kutz, F. ; Wirtz Martin, M. A. ; Meiser, N. ; Linhard, V. ; Pyper, D. J. ; Trucks, S. ; Fürtig, B. ; Hengesbach, M. ; Löhr, F. ; Richter, C. ; Saxena, K. ; Schlundt, A. ; Schwalbe, H. ; Sreeramulu, S. ; Wacker, A. ; Weigand, Julia E. ; Wirmer-Bartoschek, J. ; Wöhnert, J. |
| Art des Eintrags: | Bibliographie |
| Titel: | 1H, 13C, and 15N backbone chemical shift assignments of coronavirus-2 non-structural protein Nsp10 |
| Sprache: | Englisch |
| Publikationsjahr: | 7 November 2020 |
| Verlag: | Springer |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Biomolecular NMR assignments |
| Jahrgang/Volume einer Zeitschrift: | 2020 |
| DOI: | 10.1007/s12104-020-09984-1 |
| URL / URN: | https://link.springer.com/article/10.1007/s12104-020-09984-1... |
| Kurzbeschreibung (Abstract): | The international Covid19-NMR consortium aims at the comprehensive spectroscopic characterization of SARS-CoV-2 RNA elements and proteins and will provide NMR chemical shift assignments of the molecular components of this virus. The SARS-CoV-2 genome encodes approximately 30 different proteins. Four of these proteins are involved in forming the viral envelope or in the packaging of the RNA genome and are therefore called structural proteins. The other proteins fulfill a variety of functions during the viral life cycle and comprise the so-called non-structural proteins (nsps). Here, we report the near-complete NMR resonance assignment for the backbone chemical shifts of the non-structural protein 10 (nsp10). Nsp10 is part of the viral replication-transcription complex (RTC). It aids in synthesizing and modifying the genomic and subgenomic RNAs. Via its interaction with nsp14, it ensures transcriptional fidelity of the RNA-dependent RNA polymerase, and through its stimulation of the methyltransferase activity of nsp16, it aids in synthesizing the RNA cap structures which protect the viral RNAs from being recognized by the innate immune system. Both of these functions can be potentially targeted by drugs. Our data will aid in performing additional NMR-based characterizations, and provide a basis for the identification of possible small molecule ligands interfering with nsp10 exerting its essential role in viral replication. |
| ID-Nummer: | pmid:33159807 |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > RNA Biochemie |
| Hinterlegungsdatum: | 05 Mär 2021 08:33 |
| Letzte Änderung: | 17 Jan 2022 14:45 |
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