The Highly Flexible Disordered Regions of the SARS-CoV-2 Nucleocapsid N Protein Within the 1–248 Residue Construct: Sequence-specific Resonance Assignments through NMR
SARS-CoV-2, Covid-19, Nucleocapsid protein, NMR spectroscopy, 13C detection, IDPs
The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure as can be inferred by bioinformatics analyses as well as from the data available for the homologous protein from SARS-CoV. The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1–248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein.
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Citation / Publisher Attribution
Biomolecular NMR Assignments, v. 15, p. 219-227
Scholar Commons Citation
Schiavina, Marco; Pontoriero, Letizia; Uversky, Vladimir N.; Felli, Isabella C.; and Pierattelli, Roberta, "The Highly Flexible Disordered Regions of the SARS-CoV-2 Nucleocapsid N Protein Within the 1–248 Residue Construct: Sequence-specific Resonance Assignments through NMR" (2021). All publications. 106.