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- Title
The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
- Authors
Chang, Chung-ke; Sue, Shih-Che; Yu, Tsan-hung; Hsieh, Chiu-Min; Tsai, Cheng-Kun; Chiang, Yen-Chieh; Lee, Shin-jye; Hsiao, Hsin-hao; Wu, Wen-Jin; Chang, Chi-Fon; Huang, Tai-huang
- Abstract
Abstract: We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five α helices and a β-hairpin. The dimer interface consists of a continuous four-stranded β-sheet superposed by two long α helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the β-sheet and the α helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.
- Subjects
VIRUSES; DISEASES; HYDROGEN; TOPOLOGY
- Publication
FEBS Letters, 2005, Vol 579, Issue 25, p5663
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.09.038