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PDBsum entry 3h4z
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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 structure of the dust mite allergen der p 7 reveals similarities to innate immune proteins.
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Authors
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G.A.Mueller,
L.L.Edwards,
J.J.Aloor,
M.B.Fessler,
J.Glesner,
A.Pomés,
M.D.Chapman,
R.E.London,
L.C.Pedersen.
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Ref.
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J Allergy Clin Immunol, 2010,
125,
909.
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PubMed id
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Abstract
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BACKGROUND: Sensitization to house dust mite allergens is strongly correlated
with asthma. Der p 7 elicits strong IgE antibody and T-cell responses in
patients with mite allergy. However, the structure and biological function of
this important allergen are unknown. Allergen function might contribute to
allergenicity, as shown for the protease activity of group 1 mite allergens and
the interaction with the innate immune system by group 2 mite allergens.
OBJECTIVE: We sought to determine the crystal structure of Der p 7 and to
investigate its biological function. METHODS: X-ray crystallography was used to
determine the Der p 7 structure. Nuclear magnetic resonance analysis and
biochemical assays were used to examine the binding of Der p 7 to predicted
ligands. RESULTS: Der p 7 has an elongated structure, with two 4-stranded
antiparallel beta-sheets that wrap around a long C-terminal helix. The fold of
Der p 7 is similar to that of LPS-binding protein (LBP), which interacts with
Toll-like receptors after binding LPS and other bacterially derived lipid
ligands. Nuclear magnetic resonance and biochemical assays indicate that Der p 7
does not bind LPS but binds with weak affinity to the bacterial lipopeptide
polymyxin B in the predicted binding site of Der p 7. CONCLUSIONS: Der p 7 binds
a bacterially derived lipid product, a common feature of some allergens. The
finding that the group 7, as well as the group 2, mite allergens are
structurally similar to different proteins in the Toll-like receptor pathway
further strengthens the connections between dust mites, innate immunity, and
allergy.
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