| Literature DB >> 33660218 |
Marco Schiavina1,2, Letizia Pontoriero1,2, Vladimir N Uversky3, Isabella C Felli4,5, Roberta Pierattelli6,7.
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.Entities:
Keywords: 13C detection; Covid-19; IDPs; NMR spectroscopy; Nucleocapsid protein; SARS-CoV-2
Mesh:
Substances:
Year: 2021 PMID: 33660218 PMCID: PMC7928198 DOI: 10.1007/s12104-021-10009-8
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746