Publication Abstract from PubMed
The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: FcRI and CD23. FcRI 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 C3 and C4 domains (Fc3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fc3-4 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.
A range of C3-C4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.,Dhaliwal B, Pang MO, Yuan D, Beavil AJ, Sutton BJ Acta Crystallogr F Struct Biol Commun. 2014 Mar;70(Pt 3):305-9. doi:, 10.1107/S2053230X14003355. Epub 2014 Feb 20. PMID:24598915[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
