Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
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DOI：
10.1016/s1097-2765(00)80159-8
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发表时间：
1998-11-01
期刊：
影响因子：
16
通讯作者：
Wiley, DC
中科院分区：
文献类型：
--
作者：
Weissenhorn, W;Carfi, A;Wiley, DC
我们已经确定了埃博拉病毒膜融合糖蛋白GP2的结构，通过X射线晶体学。该分子包含一个中心三链卷曲螺旋，随后是一个与逆转录病毒糖蛋白中的免疫抑制序列同源的二硫键环，其反转链方向并连接到与核心螺旋反向平行的α螺旋。该结构表明，N末端附近的融合肽在分子的一端形成二硫键结合的环，并且C末端膜锚定在同一端。在这种构象中，GP2可以桥接两个膜并促进它们的并置以启动膜融合。我们还发现了一个七肽的不规则性，如在低pH值诱导的流感HA2和溶剂离子被困在一个卷曲的线圈，如在逆转录病毒TM。
We have determined the structure of GP2 from the Ebola virus membrane fusion glycoprotein by X-ray crystallography. The molecule contains a central triple-stranded coiled coil followed by a disulfide-bonded loop homologous to an immunosuppressive sequence in retroviral glycoproteins, which reverses the chain direction and connects to an a helix packed antiparallel to the core helices. The structure suggests that fusion peptides near the N termini form disulfide-bonded loops at one end of the molecule and that the C-terminal membrane anchors are at the same end. In this conformation, GP2 could both bridge two membranes and facilitate their apposition to initiate membrane fusion. We also find a heptad irregularity like that in low-pH-induced influenza HA2 and a solvent ion trapped in a coiled coil like that in retroviral TMs.