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|Title:||Functional and structural studies of Coronavirus ribonucleocapsid assembly||Authors:||Fan, Hui||Keywords:||DRNTU::Science::Biological sciences::Microbiology::Virology||Issue Date:||2007||Source:||Fan, H. (2007). Functional and structural studies of Coronavirus ribonucleocapsid assembly. Doctoral thesis, Nanyang Technological University, Singapore.||Abstract:||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.||URI:||https://hdl.handle.net/10356/6573||DOI:||10.32657/10356/6573||Rights:||Nanyang Technological University||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Theses|
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