Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1.

Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1.
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DOI:
10.1038/ncomms5874
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发表时间:
2014-09-16
影响因子:
16.6
通讯作者:
Stuart, David I.
Stuart, David I.
中科院分区:
综合性期刊1区
文献类型:
--
作者:
El Omari, Kamel;Iourin, Oleg;Kadlec, Jan;Sutton, Geoff;Harlos, Karl;Grimes, Jonathan M.;Stuart, David I.

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丙型肝炎病毒(HCV)感染仍然是世界范围内的一个主要卫生问题。HCV通过两种包膜糖蛋白E1和E2进入宿主细胞并实现膜融合。我们在这里报道了HCV E1外域的n端结构域的3.5-Å分辨率晶体结构,它揭示了一个共价连接的相互交织的同二聚体的复杂网络,不包含预期的截断II类融合蛋白折叠。丙型肝炎病毒(HCV)通过包膜糖蛋白E1和E2进入宿主细胞。在这里,El Omari等人展示了HCV E1外畴N端的晶体结构,并表明它采用了与预测不同的折叠。
Hepatitis C virus (HCV) infection remains a major health problem worldwide. HCV entry into host cells and membrane fusion are achieved by two envelope glycoproteins, E1 and E2. We report here the 3.5-Å resolution crystal structure of the N-terminal domain of the HCV E1 ectodomain, which reveals a complex network of covalently linked intertwined homodimers that do not harbour the expected truncated class II fusion protein fold. Hepatitis C virus (HCV) gains entry into host cells via envelope glycoproteins E1 and E2. Here, El Omari et al. present the crystal structure of the N terminus of the E1 ectodomain of HCV and show that it adopts a different fold than predicted.
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