1H, 13C and 15N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein.
Biomol NMR Assign
; 15(2): 255-260, 2021 10.
Article
in English
| MEDLINE | ID: covidwho-1453890
ABSTRACT
The nucleoprotein (N) from SARS-CoV-2 is an essential cofactor of the viral replication transcription complex and as such represents an important target for viral inhibition. It has also been shown to colocalize to the transcriptase-replicase complex, where many copies of N decorate the viral genome, thereby protecting it from the host immune system. N has also been shown to phase separate upon interaction with viral RNA. N is a 419 amino acid multidomain protein, comprising two folded, RNA-binding and dimerization domains spanning residues 45-175 and 264-365 respectively. The remaining 164 amino acids are predicted to be intrinsically disordered, but there is currently no atomic resolution information describing their behaviour. Here we assign the backbone resonances of the first two intrinsically disordered domains (N1, spanning residues 1-44 and N3, spanning residues 176-263). Our assignment provides the basis for the identification of inhibitors and functional and interaction studies of this essential protein.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Viral Proteins
/
Nuclear Magnetic Resonance, Biomolecular
/
SARS-CoV-2
/
Nucleoproteins
Type of study:
Prognostic study
Language:
English
Journal:
Biomol NMR Assign
Journal subject:
Molecular Biology
/
Nuclear Medicine
Year:
2021
Document Type:
Article
Affiliation country:
S12104-021-10014-x
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