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A range of C epsilon 3-C epsilon 4 interdomain angles in IgE Fc accommodate binding to its receptor CD23

Research output: Contribution to journalArticlepeer-review

Original languageEnglish
Article numberN/A
Pages (from-to)305-309
Number of pages5
JournalActa Crystallographica Section F-Structural Biology And Crystallization Communications
Issue number3
PublishedMar 2014

King's Authors


The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: Fc epsilon RI and CD23. Fc epsilon RI 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 C epsilon 3 and C epsilon 4 domains (Fc epsilon 3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fc epsilon 3-4 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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