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. 2005 Oct 14;13(1):59–72. doi: 10.1007/s11373-005-9035-9

Modular organization of SARS coronavirus nucleocapsid protein

Chung-ke Chang 1, Shih-Che Sue 1, Tsan-hung Yu 1, Chiu-Min Hsieh 1, Cheng-Kun Tsai 1,2, Yen-Chieh Chiang 3, Shin-jye Lee 1, Hsin-hao Hsiao 1, Wen-Jin Wu 1, Wei-Lun Chang 4, Chun-Hung Lin 4, Tai-huang Huang 1,2,✉
PMCID: PMC7089556  PMID: 16228284

Abstract

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.

Key words: capsid protein, coronavirus, domain arrangement, intrinsically disordered protein, NMR, oligomerization, SARS

Acknowledgements

This work was supported in part by the Academia Sinica and by grants (NSC 92-2113-M-001-056 and NSC 92-2751-B-001-020-Y) (to THH) from the National Science Council of the Republic of China. The NMR spectra were obtained at the High-field Biomacromolecular NMR Core Facility, National Research Program for Genomic Medicine (NRPGM), Taiwan, Republic of China.

Footnotes

CK Chang and SC Sue contributed equally to this project.

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