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

• Published in: Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2014-03, Vol.70 (3), p.305-309
• Main Authors: Dhaliwal, Balvinder, Pang, Marie O. Y., Yuan, Daopeng, Beavil, Andrew J., Sutton, Brian J.
• Format: Article
• Language: English
• Subjects: Structural Communications
• ISSN: 2053-230X; 2053-230X
• DOI: 10.1107/S2053230X14003355

The structure of a new crystal form of IgE-Fc in complex with its B-cell receptor CD23 has been determined. The structure reveals that there is conformational variability at the interface in both IgE-Fc and CD23. The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: Fc∊RI and CD23. Fc∊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∊3 and C∊4 domains (Fc∊3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23–Fc∊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.