ArticleActa crystallographica. Section F, Structural biology communications2014
A range of Cℇ3-Cℇ4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Antibodies targeting a shared epitope exploit IgE allostery to drive distinct functional outcomes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- On the complexity of IgE: The role of structural flexibility and glycosylation for binding its receptors.Frontiers in allergy · 2023Review
- Reviving lost binding sites: Exploring calcium-binding site transitions between human and murine CD23.FEBS open bio · 2021Article
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- IgE Antibodies: From Structure to Function and Clinical Translation.Antibodies (Basel, Switzerland) · 2019Review
- Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.Scientific reports · 2018Article
- Thermal sensitivity and flexibility of the Cε3 domains in immunoglobulin E.Biochimica et biophysica acta. Proteins and proteomics · 2017Article
- Allosteric mechanism of action of the therapeutic anti-IgE antibody omalizumab.The Journal of biological chemistry · 2017Article
- IgE binds asymmetrically to its B cell receptor CD23.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: FcℇRI and CD23. FcℇRI 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 Cℇ3 and Cℇ4 domains (Fcℇ3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fcℇ3-4 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.