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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 | Schools: | School of Biological Sciences | Rights: | Nanyang Technological University | Fulltext Permission: | open | Fulltext Availability: | With Fulltext |
Appears in Collections: | SBS Theses |
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SBS-THESES_2.pdf | 6.35 MB | Adobe PDF | View/Open |
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