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.
中科院分区:
文献类型:
--
作者:
El Omari, Kamel;Iourin, Oleg;Kadlec, Jan;Sutton, Geoff;Harlos, Karl;Grimes, Jonathan M.;Stuart, David I.
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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影响因子:
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