4ki1
From Proteopedia
Primitive triclinic crystal form of the human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23
Structural highlights
FunctionFCER2_HUMAN Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B-cells (it is a B-cell-specific antigen). Publication Abstract from PubMedThe 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. Loading citation details.. Citations No citations found See AlsoReferences
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