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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.
Schiavina, Marco; Pontoriero, Letizia; Uversky, Vladimir N; Felli, Isabella C; Pierattelli, Roberta.
  • Schiavina M; Magnetic Resonance Center - CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, FI, Italy.
  • Pontoriero L; Department of Chemistry "Ugo Schiff", University of Florence, Via della Lastruccia 3-13, 50019, Sesto Fiorentino, FI, Italy.
  • Uversky VN; Magnetic Resonance Center - CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, FI, Italy.
  • Felli IC; Department of Chemistry "Ugo Schiff", University of Florence, Via della Lastruccia 3-13, 50019, Sesto Fiorentino, FI, Italy.
  • Pierattelli R; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, 33612, USA.
Biomol NMR Assign ; 15(1): 219-227, 2021 04.
Article in English | MEDLINE | ID: covidwho-1384623
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Coronavirus Nucleocapsid Proteins / SARS-CoV-2 Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-021-10009-8

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Magnetic Resonance Spectroscopy / Coronavirus Nucleocapsid Proteins / SARS-CoV-2 Language: English Journal: Biomol NMR Assign Journal subject: Molecular Biology / Nuclear Medicine Year: 2021 Document Type: Article Affiliation country: S12104-021-10009-8