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PDBsum entry 1t8d
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Immune system
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PDB id
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1t8d
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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 human cd23 and its interactions with ige and cd21.
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Authors
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R.G.Hibbert,
P.Teriete,
G.J.Grundy,
R.L.Beavil,
R.Reljic,
V.M.Holers,
J.P.Hannan,
B.J.Sutton,
H.J.Gould,
J.M.Mcdonnell.
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Ref.
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J Exp Med, 2005,
202,
751-760.
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PubMed id
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Abstract
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The low-affinity immunoglobulin E (IgE) receptor, CD23 (FcepsilonRII), binds
both IgE and CD21 and, through these interactions, regulates the synthesis of
IgE, the antibody isotype that mediates the allergic response. We have
determined the three-dimensional structure of the C-type lectin domain of CD23
in solution by nuclear magnetic resonance spectroscopy. An analysis of
concentration-dependent chemical shift perturbations have allowed us to identify
the residues engaged in self-association to the trimeric state, whereas
ligand-induced changes have defined the binding sites for IgE and CD21. The
results further reveal that CD23 can bind both ligands simultaneously. Despite
the C-type lectin domain structure, none of the interactions require calcium. We
also find that IgE and CD23 can interact to form high molecular mass multimeric
complexes. The interactions that we have described provide a solution to the
paradox that CD23 is involved in both up- and down-regulation of IgE and provide
a structural basis for the development of inhibitors of allergic disease.
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