1H, 13C and 15N backbone chemical shift assignments of SARS-CoV-2 nsp3a.
Biomol NMR Assign
; 15(1): 173-176, 2021 04.
Article
in English
| MEDLINE | ID: covidwho-1043969
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
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Magnetic Resonance Spectroscopy
/
Coronavirus Papain-Like Proteases
/
SARS-CoV-2
Language:
English
Journal:
Biomol NMR Assign
Journal subject:
Molecular Biology
/
Nuclear Medicine
Year:
2021
Document Type:
Article
Affiliation country:
S12104-020-10001-8
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