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
Marco Schiavina, Letizia Pontoriero, Vladimir N. Uversky, Isabella C. Felli, Roberta Pierattelli
Abstract
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.