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PDBsum entry 4ki1
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Immune system
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PDB id
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4ki1
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References listed in PDB file
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Key reference
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Title
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A range of cℇ3-Cℇ4 interdomain angles in ige fc accommodate binding to its receptor cd23.
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Authors
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B.Dhaliwal,
M.O.Pang,
D.Yuan,
A.J.Beavil,
B.J.Sutton.
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Ref.
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Acta Crystallogr F Struct Biol Commun, 2014,
70,
305-309.
[DOI no: ]
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PubMed id
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Abstract
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The antibody IgE plays a central role in allergic disease, functioning
principally through two cell-surface receptors: FcℇRI and CD23. FcℇRI on
mast cells and basophils mediates the immediate hypersensitivity response,
whilst the interaction of IgE with CD23 on B cells regulates IgE production.
Crystal structures of the lectin-like `head' domain of CD23 alone and bound to a
subfragment of IgE consisting of the dimer of Cℇ3 and Cℇ4 domains (Fcℇ3-4)
have recently been determined, revealing flexibility in the IgE-binding site of
CD23. Here, a new crystal form of the CD23-Fcℇ3-4 complex with different
molecular-packing constraints is reported, which together with the earlier
results demonstrates that conformational variability at the interface extends
additionally to the IgE Fc and the quaternary structure of its domains.
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