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PDBsum entry 3c6e
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Viral protein
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PDB id
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3c6e
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References listed in PDB file
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Key reference
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Title
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The flavivirus precursor membrane-Envelope protein complex: structure and maturation.
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Authors
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L.Li,
S.M.Lok,
I.M.Yu,
Y.Zhang,
R.J.Kuhn,
J.Chen,
M.G.Rossmann.
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Ref.
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Science, 2008,
319,
1830-1834.
[DOI no: ]
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PubMed id
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Abstract
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Many viruses go through a maturation step in the final stages of assembly before
being transmitted to another host. The maturation process of flaviviruses is
directed by the proteolytic cleavage of the precursor membrane protein (prM),
turning inert virus into infectious particles. We have determined the 2.2
angstrom resolution crystal structure of a recombinant protein in which the
dengue virus prM is linked to the envelope glycoprotein E. The structure
represents the prM-E heterodimer and fits well into the cryo-electron microscopy
density of immature virus at neutral pH. The pr peptide beta-barrel structure
covers the fusion loop in E, preventing fusion with host cell membranes. The
structure provides a basis for identifying the stages of its pH-directed
conformational metamorphosis during maturation, ending with release of pr when
budding from the host.
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Figure 2.
Fig. 2. Rearrangement of the prM and E proteins during virus
maturation. (A to D) Sequence of events as referenced in the
text. The E proteins are shown as a C  backbone;
space-filling atoms show the pr peptide surfaces. The three
independent heterodimers per icosahedral asymmetric unit are
colored red, green, and blue. Although the diagram assumes
knowledge of the relationship among the positions of specific
heterodimers in the immature and mature viruses (red goes to
red, green to green, and blue to blue), this is not known.
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Figure 3.
Fig. 3. Structure of the prM-E protein. (A)Stereoview of the
prM-E heterodimer in ribbon representation. The pr peptide is
cyan, DI is red, DII is yellow, DIII is blue, and the fusion
loop is green. Secondary structural elements of the E protein
are labeled (7, 21). Secondary structural elements for the pr
peptide are defined here as a[pr], b[pr],
···, g[pr]. (B) Secondary structure of the
pr peptide. Disulfide linkages are indicated with dashed lines.
(C) Open-book view of the pr-E interactions showing charge
complementarity. Positively and negatively charged surfaces in
the contact areas are colored blue and red, respectively.
Charged residues in the contact area are labeled. The fusion
loop (residues 100 to 108) is outlined in green. Contact areas
are defined by atoms less than 4.5 Å apart between the pr
peptide and the E protein (21).
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The above figures are
reprinted
by permission from the AAAs:
Science
(2008,
319,
1830-1834)
copyright 2008.
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