Abstract |
The causative agent of severe acute respiratory syndrome (SARS) is the SARS-associated coronavirus, SARS-CoV. The nucleocapsid (N) protein plays an essential role in SARS-CoV genome packaging and virion assembly. We have previously shown that SARS-CoV N protein forms a dimer in solution through its C-terminal domain. In this study, the crystal structure of the dimerization domain, consisting of residues 270-370, is determined to 1.75A resolution. The structure shows a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo. Although lacking significant sequence similarity, the dimerization domain of SARS-CoV N protein has a fold similar to that of the nucleocapsid protein of the porcine reproductive and respiratory syndrome virus. This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin.
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Authors | I-Mei Yu, Michael L Oldham, Jingqiang Zhang, Jue Chen |
Journal | The Journal of biological chemistry
(J Biol Chem)
Vol. 281
Issue 25
Pg. 17134-17139
(Jun 23 2006)
ISSN: 0021-9258 [Print] United States |
PMID | 16627473
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
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Chemical References |
- Coronavirus Nucleocapsid Proteins
- Nucleocapsid Proteins
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Topics |
- Amino Acid Sequence
- Arteriviridae
(genetics)
- Coronavirus Nucleocapsid Proteins
- Crystallography, X-Ray
- Dimerization
- Evolution, Molecular
- Molecular Sequence Data
- Nucleocapsid Proteins
(chemistry)
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary
- Severe acute respiratory syndrome-related coronavirus
(genetics, metabolism)
- Sequence Homology, Amino Acid
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