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PDBsum entry 3d34
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Immune system
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PDB id
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3d34
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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 the f-Spondin domain of mindin, An integrin ligand and pattern recognition molecule.
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Authors
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Y.Li,
C.Cao,
W.Jia,
L.Yu,
M.Mo,
Q.Wang,
Y.Huang,
J.M.Lim,
M.Ishihara,
L.Wells,
P.Azadi,
H.Robinson,
Y.W.He,
L.Zhang,
R.A.Mariuzza.
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Ref.
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Embo J, 2009,
28,
286-297.
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PubMed id
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Abstract
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Mindin (spondin-2) is an extracellular matrix protein of unknown structure that
is required for efficient T-cell priming by dendritic cells. Additionally,
mindin functions as a pattern recognition molecule for initiating innate immune
responses. These dual functions are mediated by interactions with integrins and
microbial pathogens, respectively. Mindin comprises an N-terminal F-spondin (FS)
domain and C-terminal thrombospondin type 1 repeat (TSR). We determined the
structure of the FS domain at 1.8-A resolution. The structure revealed an
eight-stranded antiparallel beta-sandwich motif resembling that of
membrane-targeting C2 domains, including a bound calcium ion. We demonstrated
that the FS domain mediates integrin binding and identified the binding site by
mutagenesis. The mindin FS domain therefore represents a new integrin ligand. We
further showed that mindin recognizes lipopolysaccharide (LPS) through its TSR
domain, and obtained evidence that C-mannosylation of the TSR influences LPS
binding. Through these dual interactions, the FS and TSR domains of mindin
promote activation of both adaptive and innate immune responses.
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