Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/6573
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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