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PDBsum entry 2b6b
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Virus/receptor
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PDB id
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2b6b
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References listed in PDB file
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Key reference
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Title
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Cryo-Em reconstruction of dengue virus in complex with the carbohydrate recognition domain of dc-Sign.
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Authors
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E.Pokidysheva,
Y.Zhang,
A.J.Battisti,
C.M.Bator-Kelly,
P.R.Chipman,
C.Xiao,
G.G.Gregorio,
W.A.Hendrickson,
R.J.Kuhn,
M.G.Rossmann.
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Ref.
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Cell, 2006,
124,
485-493.
[DOI no: ]
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PubMed id
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Abstract
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Dengue virus (DENV) is a significant human pathogen that causes millions of
infections and results in about 24,000 deaths each year. Dendritic cell-specific
ICAM3 grabbing nonintegrin (DC-SIGN), abundant in immature dendritic cells, was
previously reported as being an ancillary receptor interacting with the surface
of DENV. The structure of DENV in complex with the carbohydrate recognition
domain (CRD) of DC-SIGN was determined by cryo-electron microscopy at 25 A
resolution. One CRD monomer was found to bind to two glycosylation sites at
Asn67 of two neighboring glycoproteins in each icosahedral asymmetric unit,
leaving the third Asn67 residue vacant. The vacancy at the third Asn67 site is a
result of the nonequivalence of the glycoprotein environments, leaving space for
the primary receptor binding to domain III of E. The use of carbohydrate
moieties for receptor binding sites suggests a mechanism for avoiding immune
surveillance.
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Figure 1.
Figure 1. Structure of DC-SIGN
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Figure 3.
Figure 3. Diagrammatic Representation of a DC-SIGN
Tetrameric Molecule Interacting with the DENV Surface
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
124,
485-493)
copyright 2006.
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Headers
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