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Publication Abstract from PubMed

The antibody IgE plays a central role in allergic disease mechanisms. Its effector functions are controlled through interactions between the Fc region and two principal cell surface receptors FcepsilonRI and CD23. The interaction with FcepsilonRI is primarily responsible for allergic sensitization and the inflammatory response, while IgE binding to CD23 is involved in the regulation of IgE synthesis and allergen transcytosis. Here we present the crystal structure of a CD23/IgE-Fc complex and conduct isothermal titration calorimetric binding studies. Two lectin-like "head" domains of CD23 bind to IgE-Fc with affinities that differ by more than an order of magnitude, but the crystal structure reveals only one head bound to one of the two identical heavy-chains in the asymmetrically bent IgE-Fc. These results highlight the subtle interplay between receptor binding sites in IgE-Fc and their affinities, the understanding of which may be exploited for therapeutic intervention in allergic disease.

IgE binds asymmetrically to its B cell receptor CD23.,Dhaliwal B, Pang MO, Keeble AH, James LK, Gould HJ, McDonnell JM, Sutton BJ, Beavil AJ Sci Rep. 2017 Mar 31;7:45533. doi: 10.1038/srep45533. PMID:28361904^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.