Wiley, Acta Crystallographica Section a Foundations of Crystallography, s1(58), p. c6-c6, 2002
DOI: 10.1107/s0108767302085343
Elsevier, Cell, 5(108), p. 717-725, 2002
DOI: 10.1016/s0092-8674(02)00660-8
Selected Papers of Michael G Rossmann with Commentaries, p. 317-325
DOI: 10.1142/9789814513357_0037
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The first structure of a flavivirus has been determined by using a comThe 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 β barrels of domain II of the glycoprotein E are inserted into the cellular membrane.