1 H, 13 C and 15 N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein

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...

Full description

Saved in:
Bibliographic Details
Published inBiomolecular NMR assignments Vol. 15; no. 2; p. 255
Main Authors Guseva, Serafima, Perez, Laura Mariño, Camacho-Zarco, Aldo, Bessa, Luiza Mamigonian, Salvi, Nicola, Malki, Anas, Maurin, Damien, Blackledge, Martin
Format Journal Article
LanguageEnglish
Published Netherlands 01.10.2021
Subjects
Carbon Isotopes
Coronavirus Nucleocapsid Proteins - chemistry
Intrinsically Disordered Proteins - chemistry
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Nucleocapsid Proteins - chemistry
Nucleoproteins - chemistry
Phosphoproteins
Protein Domains
Protein Structure, Secondary
SARS-CoV-2
COVID-19
Relaxation
NMR
SARS-CoV-2
Dynamics
Nucleoprotein
Intrinsically disordered protein
Online AccessGet full text

Cover

More Information
Summary: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.
ISSN:1874-270X