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Biomol NMR Assign . 1 H, 13 C, and 15 N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e

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  • Biomol NMR Assign . 1 H, 13 C, and 15 N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e


    Biomol NMR Assign


    . 2020 Aug 8.
    doi: 10.1007/s12104-020-09971-6. Online ahead of print.
    1 H, 13 C, and 15 N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e


    Sophie M Korn 1 2 , Karthikeyan Dhamotharan 1 2 , Boris Fürtig 3 2 , Martin Hengesbach 3 2 , Frank Löhr 4 2 , Nusrat S Qureshi 3 2 , Christian Richter 3 2 , Krishna Saxena 3 2 , Harald Schwalbe 3 2 , Jan-Niklas Tants 1 2 , Julia E Weigand 5 , Jens Wöhnert 1 2 , Andreas Schlundt 6 7



    Affiliations

    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.

    Keywords: Covid19-NMR; Non-structural protein; Nucleic acid-binding domain; Protein drugability; SARS-CoV-2; Solution NMR-spectroscopy.

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