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Contents |
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* Residue conservation analysis
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DOI no:
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Mol Cell
8:169-179
(2001)
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PubMed id:
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Herpes simplex virus glycoprotein D bound to the human receptor HveA.
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A.Carfí,
S.H.Willis,
J.C.Whitbeck,
C.Krummenacher,
G.H.Cohen,
R.J.Eisenberg,
D.C.Wiley.
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ABSTRACT
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Herpes simplex virus (HSV) infection requires binding of the viral envelope
glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of
a soluble, truncated ectodomain of gD both alone and in complex with the
ectodomain of its cellular receptor HveA. Two bound anions suggest possible
binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate.
Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the
core of gD that is closely related to cellular adhesion molecules and flanked by
large N- and C-terminal extensions. The receptor binding segment of gD, an
N-terminal hairpin, appears conformationally flexible, suggesting that a
conformational change accompanying binding might be part of the viral entry
mechanism.
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Selected figure(s)
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Figure 3.
Figure 3. The gD-HveA Interface
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Figure 5.
Figure 5. Conformational Change in the N
Terminus of gD
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2001,
8,
169-179)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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 |
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