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PDBsum entry 4gjt
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Membrane protein/viral protein
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PDB id
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4gjt
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References listed in PDB file
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Key reference
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Title
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Structure of measles virus hemagglutinin bound to its epithelial receptor nectin-4.
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Authors
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X.Zhang,
G.Lu,
J.Qi,
Y.Li,
Y.He,
X.Xu,
J.Shi,
C.W.Zhang,
J.Yan,
G.F.Gao.
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Ref.
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Nat Struct Biol, 2013,
20,
67-72.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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Measles virus is a major public health concern worldwide. Three measles virus
cell receptors have been identified so far, and the structures of the first two
in complex with measles virus hemagglutinin (MV-H) have been reported. Nectin-4
is the most recently identified receptor in epithelial cells, and its binding
mode to MV-H remains elusive. In this study, we solved the structure of the
membrane-distal domain of human nectin-4 in complex with MV-H. The structure
shows that nectin-4 binds the MV-H β4-β5 groove exclusively via its N-terminal
IgV domain; the contact interface is dominated by hydrophobic interactions. The
binding site in MV-H for nectin-4 also overlaps extensively with those of the
other two receptors. Finally, a hydrophobic pocket centered in the β4-β5
groove is involved in binding to all three identified measles virus receptors,
representing a potential target for antiviral drugs.
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