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

Biomol NMR Assign. 2021 Apr;15(1):173-176. doi: 10.1007/s12104-020-10001-8. Epub 2021 Jan 21.

Abstract

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.

Keywords: Covid-19; Intrinsically disordered protein; SARS-CoV-2; Viral replication.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes
  • Coronavirus Papain-Like Proteases / chemistry*
  • Escherichia coli
  • Hydrogen
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy*
  • Nitrogen Isotopes
  • Plasmids / metabolism
  • Protein Binding
  • Protein Domains
  • Protein Structure, Secondary
  • SARS-CoV-2 / chemistry*

Substances

  • Carbon Isotopes
  • Nitrogen Isotopes
  • Nitrogen-15
  • Hydrogen
  • Coronavirus Papain-Like Proteases
  • papain-like protease, SARS-CoV-2
  • Carbon-13