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The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus‐like structure
Author(s) -
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
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.038
Subject(s) - dimer , porcine reproductive and respiratory syndrome virus , coronavirus , hydrogen bond , crystallography , protein structure , virology , chemistry , covid-19 , beta sheet , virus , viral protein , peptide sequence , protein secondary structure , biology , molecule , gene , biochemistry , medicine , disease , organic chemistry , pathology , infectious disease (medical specialty)
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.