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

Nicola Salvi, Luiza Mamigonian Bessa, Serafima Guseva, Aldo Camacho-Zarco, Damien Maurin, Laura Marino Perez, Anas Malki, Martin Hengesbach, Sophie Marianne Korn, Andreas Schlundt, Harald Schwalbe, Martin Blackledge

Research output: Contribution to journalArticlepeer-review

Abstract

© 2021, The Author(s), under exclusive licence to Springer Nature B.V. part of Springer Nature. 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.
Original languageEnglish
JournalBiomolecular NMR Assignments
DOIs
StatePublished - 1 Jan 2021

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