1p58: Difference between revisions

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[[Image:1p58.gif|left|200px]]
{{Seed}}
[[Image:1p58.png|left|200px]]


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{{STRUCTURE_1p58|  PDB=1p58  |  SCENE=  }}  
{{STRUCTURE_1p58|  PDB=1p58  |  SCENE=  }}  


'''Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction'''
===Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_14528291}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_14528291}}


==About this Structure==
==About this Structure==
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[[Category: Icosahedral virus]]
[[Category: Icosahedral virus]]
[[Category: Membrane protein m]]
[[Category: Membrane protein m]]
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