ArticleNature structural & molecular biology2014
Human immunoglobulin E flexes between acutely bent and extended conformations.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
31 citing papers in PubMed, 62 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
- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- Long-range allosteric communication within antibodies affects antigen-binding affinity.Frontiers in immunology · 2026Article
- Article
- Allosteric inhibition of IgE-FcεRI interactions by simultaneous targeting of IgE F(ab')2 epitopes.Communications biology · 2024Article
- The evolution of flexibility and function in the Fc domains of IgM, IgY, and IgE.Frontiers in immunology · 2024Article
- IgE Immune Complexes Mitigate Eosinophilic Immune Responses through NLRC4 Inflammasome.Mediators of inflammation · 2023Article
- Cryomicroscopy reveals the structural basis for a flexible hinge motion in the immunoglobulin M pentamer.Nature communications · 2022Article
- Tuning IgE: IgE-Associating Molecules and Their Effects on IgE-Dependent Mast Cell Reactions.Cells · 2021Review
- A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF.Nature communications · 2021Article
- Modulating Target Protein Biology Through the Re-mapping of Conformational Distributions Using Small Molecules.Frontiers in chemistry · 2021Article
- Immunoglobulins or Antibodies: IMGTBiomedicines · 2020Review
- NMR backbone assignment of the Cε4 domain of immunoglobulin E.Biomolecular NMR assignments · 2020Article
- 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
- Specific panallergen peptide of Sorghum Polcalcin showing IgE response identified based on in silico and in vivo peptide mapping.Bioscience reports · 2019Article
- IgE Antibodies: From Structure to Function and Clinical Translation.Antibodies (Basel, Switzerland) · 2019Review
- IgE repertoire and immunological memory: compartmental regulation and antibody function.International immunology · 2018Review
- Structural basis for selective inhibition of immunoglobulin E-receptor interactions by an anti-IgE antibody.Scientific reports · 2018Article
- Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction.Nature communications · 2018Article
- Immunoglobulin E-Mediated Autoimmunity.Frontiers in immunology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
Crystallographic and solution studies have shown that IgE molecules are acutely bent in their Fc region. Crystal structures reveal the Cɛ2 domain pair folded back onto the Cɛ3-Cɛ4 domains, but is the molecule exclusively bent or can the Cɛ2 domains adopt extended conformations and even 'flip' from one side of the molecule to the other? We report the crystal structure of IgE-Fc captured in a fully extended, symmetrical conformation and show by molecular dynamics, calorimetry, stopped-flow kinetic, surface plasmon resonance (SPR) and Förster resonance energy transfer (FRET) analyses that the antibody can indeed adopt such extended conformations in solution. This diversity of conformational states available to IgE-Fc offers a new perspective on IgE function in allergen recognition, as part of the B-cell receptor and as a therapeutic target in allergic disease.
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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.