El Omari Kamel, Iourin Oleg, Kadlec Jan, Sutton Geoff, Harlos Karl, Grimes Jonathan M, Stuart David I
1] Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK [2].
Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK.
Nat Commun. 2014 Sep 16;5:4874. doi: 10.1038/ncomms5874.
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.
丙型肝炎病毒（HCV）感染仍是全球主要的健康问题。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。我们在此报告HCV E1胞外域N端结构域的3.5埃分辨率晶体结构，该结构揭示了一个由共价连接的交织同型二聚体组成的复杂网络，这些同型二聚体不具有预期的截短的II类融合蛋白折叠结构。
