Sophie Korn, Karthikeyan Dhamotharan, Boris Fürtig, Martin Hengesbach, Frank Löhr, Nusrat Qureshi, Christian Richter, Krishna Saxena, Harald Schwalbe, Jan-Niklas Tants, Julia Weigand, Jens Wöhnert, Andreas Schlundt
- 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.
MetadatenAuthor: | Sophie KornORCiDGND, Karthikeyan DhamotharanORCiDGND, Boris FürtigORCiDGND, Martin HengesbachORCiDGND, Frank LöhrORCiD, Nusrat QureshiORCiDGND, Christian RichterORCiDGND, Krishna SaxenaORCiDGND, Harald SchwalbeORCiDGND, Jan-Niklas TantsORCiD, Julia WeigandORCiDGND, Jens WöhnertORCiDGND, Andreas SchlundtORCiDGND |
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URN: | urn:nbn:de:hebis:30:3-694517 |
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DOI: | https://doi.org/10.1007/s12104-020-09971-6 |
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ISSN: | 1874-270X |
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Parent Title (English): | Biomolecular NMR assignments |
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Publisher: | Springer Netherlands |
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Place of publication: | Dordrecht [u.a.] |
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Document Type: | Article |
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Language: | English |
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Date of Publication (online): | 2020/08/08 |
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Date of first Publication: | 2020/08/08 |
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Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
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Release Date: | 2023/03/06 |
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Tag: | Covid19-NMR; Non-structural protein; Nucleic acid-binding domain; Protein drugability; SARS-CoV-2; Solution NMR-spectroscopy |
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Volume: | 14 |
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Issue: | 2 |
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Page Number: | 5 |
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First Page: | 329 |
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Last Page: | 333 |
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Note: | Open Access funding provided by Projekt DEAL. The Frankfurt BMRZ (Center for Biomolecular Resonance) is supported by the Federal state of Hesse. |
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Note: | This work was funded by the Deutsche Forschungsgemeinschaft through grant numbers SFB902/B18 (to covid19-nmr), SCHL2062/2 − 1 (to A.S.), and by the Johanna Quandt Young Academy at Goethe (Grant Number 2019/AS01 to A.S.). |
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Note: | The chemical shift values for the 1H, 13C and 15N resonances of SARS-CoV-2 Nsp3e have been deposited at the BioMagResBank (https://www.bmrb.wisc.edu) under accession number 50334. Spectral raw data (upon request) and assignments are also accessible through https://covid19-nmr.de. |
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HeBIS-PPN: | 508546605 |
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Institutes: | Biochemie, Chemie und Pharmazie |
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| Biowissenschaften |
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Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften |
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| 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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Sammlungen: | Universitätspublikationen |
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Licence (German): | Creative Commons - CC BY - Namensnennung 4.0 International |
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