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COVID19-NMR

COVID19-NMR

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Publications

DOI

Biomolecular NMR Assignments (2021) 15:173–176

1H, 13C and 15N backbone chemical shift assignments of SARS-CoV-2 nsp3a

N. Salvi, L. M. Bessa, S. Guseva, A. Camacho-Zarco, D. Maurin, L. M. Perez, A. Malki, M. Hengesbach, S. M. Korn, A. Schlundt, H. Schwalbe & M. Blackledge

The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein.

Funded by


Goethe Corona Fonds

DFG

Volkswagen Stiftung

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Coordination

Prof. Dr. Harald Schwalbe (Coordinator)
Institut für Organische Chemie und Chemische Biologie
Zentrum für Biomolekulare Magnetische Resonanz

Johann Wolfgang Goethe-Universität
N160-3.13
Max-von-Laue-Strasse 7
D-60438 Frankfurt am Main

Contact us

++49 69 798 29737
schwalbe@nmr.uni-frankfurt.de

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