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-Structure paper
Title | Cryo-EM structure of the mature dengue virus at 3.5-Å resolution. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 20, Issue 1, Page 105-110, Year 2013 |
Publish date | Dec 16, 2012 |
Authors | Xiaokang Zhang / Peng Ge / Xuekui Yu / Jennifer M Brannan / Guoqiang Bi / Qinfen Zhang / Stan Schein / Z Hong Zhou / |
PubMed Abstract | Regulated by pH, membrane-anchored proteins E and M function during dengue virus maturation and membrane fusion. Our atomic model of the whole virion from cryo-electron microscopy at 3.5-Å ...Regulated by pH, membrane-anchored proteins E and M function during dengue virus maturation and membrane fusion. Our atomic model of the whole virion from cryo-electron microscopy at 3.5-Å resolution reveals that in the mature virus at neutral extracellular pH, the N-terminal 20-amino-acid segment of M (involving three pH-sensing histidines) latches and thereby prevents spring-loaded E fusion protein from prematurely exposing its fusion peptide. This M latch is fastened at an earlier stage, during maturation at acidic pH in the trans-Golgi network. At a later stage, to initiate infection in response to acidic pH in the late endosome, M releases the latch and exposes the fusion peptide. Thus, M serves as a multistep chaperone of E to control the conformational changes accompanying maturation and infection. These pH-sensitive interactions could serve as targets for drug discovery. |
External links | Nat Struct Mol Biol / PubMed:23241927 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 Å |
Structure data | |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRUS / flavivirus / fusion protein / protein complex / membrane / chaperone / VIRAL PROTEIN |