| Literature DB >> 14528291 |
Wei Zhang1, Paul R Chipman, Jeroen Corver, Peter R Johnson, Ying Zhang, Suchetana Mukhopadhyay, Timothy S Baker, James H Strauss, Michael G Rossmann, Richard J Kuhn.
Abstract
Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 A by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope (E) and 180 membrane (M) proteins in the lipid envelope. The alpha-helical 'stem' regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The 'anchor' regions of E and the M proteins each form antiparallel E-E and M-M transmembrane alpha-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus.Entities:
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Year: 2003 PMID： 14528291 PMCID： PMC4148076 DOI： 10.1038/nsb990
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368