Conformational changes of the flavivirus E glycoprotein
Conformational changes of the flavivirus E glycoprotein
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DOI：
10.1016/j.str.2004.06.019
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发表时间：
2004-09-01
期刊：
影响因子：
5.7
通讯作者：
Rossmann, MG
中科院分区：
文献类型：
--
作者：
Zhang, Y;Zhang, W;Rossmann, MG
登革病毒是黄病毒科的成员，其表面由180个拷贝的包膜（E）糖蛋白和膜（M）蛋白组成。E的N-末端片段的晶体结构已被确定，并与先前描述的结构进行比较。这些结构之间的主要区别是围绕将融合结构域DII与结构域DI和DIII相关联的铰链旋转10度。这两个刚体组件用于独立拟合E到未成熟和成熟的登革热病毒的冷冻电子显微镜图。这两种粒子的拟合E结构表明两种组分之间相差27度。融合后的E结构与未成熟和成熟病毒体的E结构的比较显示了大约围绕相同铰链的旋转。E的柔性显然是黄病毒装配和感染的功能要求。
Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10degrees rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27degrees between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses.