Crystal structure of the Mengla virus VP30 C-terminal domain
Crystal structure of the Mengla virus VP30 C-terminal domain
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勐腊病毒VP30 C端结构域的晶体结构
DOI：
10.1016/j.bbrc.2020.02.089
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发表时间：
2020
影响因子：
3.1
通讯作者：
Qin Xiaochun
中科院分区：
文献类型：
--
作者：
Dong Shishang;Wen Kangning;Chu Hongguan;Li Hui;Yu Qianqian;Wang Changhui;Qin Xiaochun
丝状病毒科包含许多重要的人类病毒，包括马尔堡病毒(Marburg Virus，MARV)和埃博拉病毒(Ebola Virus，EBOV)。Měnla病毒是一种新发现的丝状病毒，被认为是一种潜在的人类病原体。这些丝状病毒的VP30C末端结构域(CTD)在病毒粒子组装过程中起着至关重要的作用。与其他丝状病毒一样，MLAV VP30 CTD主要以二聚体形式存在于溶液中。在本工作中，我们测定了重组MLAV VP30 CTD单体的晶体结构，验证了C-末端螺旋-7(H7)在二聚过程中是关键的。本研究为MLAV VP30 CTD作为抗丝病毒药物开发靶点的研究提供了初步模型。
The family Filoviridae contains many important human viruses, including Marburg virus (MARV) and Ebola virus (EBOV). Měnglà virus (MLAV), a newly discovered filovirus, is considered a potential human pathogen. The VP30 C-terminal domain (CTD) of these filoviruses plays an essential role in virion assembly. In common with other filoviruses, MLAV VP30 CTD mainly exists as a dimer in solution. In this work, we determined the crystal structure of recombinant MLAV VP30 CTD monomer, verifying that C-terminal helix-7 (H7) is critical for the dimerization process. This study provides a preliminary model for investigation of MLAV VP30 CTD as an anti-filovirus drug development target.