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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 NMRстатья
- Авторы: Schiavina M., Pontoriero L., Uversky V.N., Felli I.C., Pierattelli R.
- Журнал: Biomolecular NMR Assignments
- Том: 15
- Номер: 1
- Год издания: 2021
- Издательство: Springer Verlag
- Местоположение издательства: Germany
- Первая страница: 219
- Последняя страница: 227
- Аннотация: 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.
- Добавил в систему: Уверский Владимир Николаевич