摘要
The SARS-CoV nucleocapsid (N) protein is a major antigen in severe acute respiratory syndrome. It binds to the viral RNA genome and forms the ribonucleoprotein core. The SARS-CoV N protein has also been suggested to be involved in other important functions in the viral life cycle. Here we show that the N protein consists of two non-interacting structural domains, the N-terminal RNA-binding domain (RBD) (residues 45-181) and the C-terminal dimerization domain (residues 248-365) (DD), surrounded by flexible linkers. The C-terminal domain exists exclusively as a dimer in solution. The flexible linkers are intrinsically disordered and represent potential interaction sites with other protein and protein-RNA partners. Bioinformatics reveal that other coronavirus N proteins could share the same modular organization. This study provides information on the domain structure partition of SARS-CoV N protein and insights into the differing roles of structured and disordered regions in coronavirus nucleocapsid proteins.
原文 | 英語 |
---|---|
頁(從 - 到) | 59-72 |
頁數 | 14 |
期刊 | Journal of Biomedical Science |
卷 | 13 |
發行號 | 1 |
DOIs | |
出版狀態 | 已發佈 - 2006 1月 |
ASJC Scopus subject areas
- 內分泌學、糖尿病和代謝
- 分子生物學
- 臨床生物化學
- 細胞生物學
- 生物化學(醫學)
- 藥學(醫學)