期刊
CELL
卷 108, 期 5, 页码 717-725出版社
CELL PRESS
DOI: 10.1016/S0092-8674(02)00660-8
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资金
- NIAID NIH HHS [AI10793, P01 AI045976, AI45976, R01 AI020612, AI20612] Funding Source: Medline
- NIGMS NIH HHS [GM08296, T32 GM008296] Funding Source: Medline
The first structure of a flavivirus has been determined by using a combination of cryoelectron microscopy and fitting of the known structure of glycoprotein E into the electron density map. The virus core, within a lipid bilayer, has a less-ordered structure than the external, icosahedral scaffold of 90 glycoprotein E dimers. The three E monomers per icosahedral asymmetric unit do not have quasiequivalent symmetric environments. Difference maps indicate the location of the small membrane protein M relative to the overlaying scaffold of E dimers. The structure suggests that flaviviruses, and by analogy also alphaviruses, employ a fusion mechanism in which the distal beta barrels of domain II of the glycoprotein E are inserted into the cellular membrane.
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