| Literature DB >> 11893341 |
Richard J Kuhn1, Wei Zhang, Michael G Rossmann, Sergei V Pletnev, Jeroen Corver, Edith Lenches, Christopher T Jones, Suchetana Mukhopadhyay, Paul R Chipman, Ellen G Strauss, Timothy S Baker, James H Strauss.
Abstract
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.Entities:
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Year: 2002 PMID: 11893341 PMCID: PMC4152842 DOI: 10.1016/s0092-8674(02)00660-8
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582