| Primary Identifier | IPR037179 | Type | Homologous_superfamily |
| Short Name | Nucleocapsid_C |
| description | The Nucleocapsid (N) protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signalling pathways. The N protein interacts with genomic and subgenomic RNA molecules. Together with the envelope protein M, it participates in genome condensation and packaging. The N protein is a highly immunogenic and abundantly expressed protein during infection, capable of inducing protective immune responses against SARS-CoV and SARS-CoV-2 [, , , , ].Coronavirus (CoV) nucleocapsid (N) proteins have 3 highly conserved domains. The N-terminal domain (NTD) (N1b), the C-terminal domain (CTD)(N2b) and the N3 region. The N1b and N2b domains from SARS CoV, infectious bronchitis virus (IBV), human CoV 229E and mouse hepatic virus (MHV) display similar topological organisations. N proteins form dimers, which are asymmetrically arranged into octamers via their N2b domains []. Both domains contribute to the binding of viral RNA genome [, ].This entry represents the C-terminal domain of the nucleocapsid proteins from Coronavirus and Arterivirus. The C-terminal domain of the N protein (N-CTD) is involved in dimerization, and is thus, also called the dimerization domain []. Structurally, the C-terminal domain forms a tightly intertwined dimer with an intermolecular four-stranded central β-sheet platform flanked by alpha helices, indicating that the basic building block for coronavirus nucleocapsid formation is a dimeric assembly of N protein []. |
