IgE binds asymmetrically to its B cell receptor CD23 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Balvinder Dhaliwal, Marie O Y Pang, Anthony H Keeble, Louisa K James, Hannah J Gould, James M McDonnell, Brian J Sutton, Andrew J Beavil

ABSTRACT

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 FcεRI and CD23. The interaction with FcεRI 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. More... »

PAGES

45533

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep45533

DOI

http://dx.doi.org/10.1038/srep45533

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1084133274

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28361904


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