Functional and structural studies of Coronavirus ribonucleocapsid assembly.
Date of Issue2007
School of Biological Sciences
Our research found that the Coronavirus infectious bronchitis virus (IBV) nucleocapsid (N) protein consists of two domains: N-terminal domain and C-terminal domain, which are connected by an arginine, serine, alanine rich linker. The N-terminal domain of the IBV N protein exhibits typical RNA-binding protein’s features, with a flexible hairpin loop rich in basic residues and a hydrophobic floor, providing a module for specific interaction with RNA. The C-terminal domain forms a tightly intertwined dimer with an intermolecular four-stranded central ?-sheet platform flanked by a helices. A possible nucleocapsid formation model was proposed that the C-terminal domain forms a helical nucleocapsid scaffold by dimerization and interdimer stacking. The N-terminal domain connects to the helical scaffold by arginine, serine, alanine rich linker and is mainly responsible for RNA binding.
Nanyang Technological University