作者: Yu-Sheng Lo , Shing-Yen Lin , Shiu-Mei Wang , Chin-Tien Wang , Ya-Li Chiu
DOI: 10.1016/J.FEBSLET.2012.11.016
关键词:
摘要: The coronavirus (CoV) N protein oligomerizes via its carboxyl terminus. However, the oligomerization mechanism of C-terminal domains (CTD) CoV proteins remains unclear. Based on disorder prediction system, a comprehensive series HCoV-229E mutants with truncated CTD was generated and systematically investigated by biophysical biochemical analyses to clarify role tail in oligomerization. These results indicate that last plays an important dimer-dimer association. peptide is able interfere performs inhibitory effect viral titre HCoV-229E. This study may assist development anti-viral drugs against HCoV.