IgE binds asymmetrically to its B cell receptor CD23.
dc.contributor.author | Dhaliwal, B | |
dc.contributor.author | Pang, MOY | |
dc.contributor.author | Keeble, AH | |
dc.contributor.author | James, LK | |
dc.contributor.author | Gould, HJ | |
dc.contributor.author | McDonnell, JM | |
dc.contributor.author | Sutton, BJ | |
dc.contributor.author | Beavil, AJ | |
dc.date.accessioned | 2019-03-12T14:37:21Z | |
dc.date.available | 2017-03-17 | |
dc.date.available | 2019-03-12T14:37:21Z | |
dc.date.issued | 2017-03-31 | |
dc.identifier.citation | Dhaliwal, B. et al. IgE binds asymmetrically to its B cell receptor CD23. Sci. Rep. 7, 45533; doi: 10.1038/srep45533 (2017). | en_US |
dc.identifier.issn | 2045-2322 | |
dc.identifier.uri | https://qmro.qmul.ac.uk/xmlui/handle/123456789/56107 | |
dc.description.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. | en_US |
dc.format.extent | 45533 | |
dc.language | eng | |
dc.language.iso | en | en_US |
dc.publisher | Nature Research (part of Springer Nature) | en_US |
dc.relation.ispartof | Sci Rep | |
dc.rights | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | |
dc.rights | Attribution 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/us/ | * |
dc.subject | Allergens | en_US |
dc.subject | B-Lymphocytes | en_US |
dc.subject | Binding Sites | en_US |
dc.subject | Humans | en_US |
dc.subject | Immunoglobulin E | en_US |
dc.subject | Immunoglobulin Fc Fragments | en_US |
dc.subject | Protein Binding | en_US |
dc.subject | Receptors, IgE | en_US |
dc.subject | Transcytosis | en_US |
dc.title | IgE binds asymmetrically to its B cell receptor CD23. | en_US |
dc.type | Article | en_US |
dc.rights.holder | © The Author(s) 2017 | |
dc.identifier.doi | 10.1038/srep45533 | |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/28361904 | en_US |
pubs.notes | No embargo | en_US |
pubs.publication-status | Published online | en_US |
pubs.publisher-url | https://doi.org/10.1038/srep45533 | |
pubs.volume | 7 | en_US |
dcterms.dateAccepted | 2017-02-21 | |
rioxxterms.funder | Default funder | en_US |
rioxxterms.identifier.project | Default project | en_US |
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Except where otherwise noted, this item's license is described as This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/