Cryo‐EM Structure of FcεRI Bound IgE Reveals Multiple Defined Conformations of the Fab‐Fc Hinge
Our data reveal the architecture of a full-size IgE antibody bound to its receptor and a new layer of dynamics in FcεRIα bound IgE on top of the well-established IgE Fc conformations. Development of novel anti-IgE therapeutics may take into account these properties of FcεRIα bound IgE.
Authors
- Edzard Spillner (ORCID: https://orcid.org/0000-0003-0999-5254)
- Martin Høgholm Jørgensen (ORCID: https://orcid.org/0000-0002-4459-5523)
- Rasmus K. Jensen (ORCID: https://orcid.org/0000-0001-5472-4862)
- Gregers Rom Andersen (ORCID: https://orcid.org/0000-0001-6292-3319)
- Rosaria Gandini (ORCID: https://orcid.org/0000-0003-4171-0693)
- Michaela Miehe (ORCID: https://orcid.org/0000-0001-6622-7230)
Institutions
- Aarhus University (DK)
- European Molecular Biology Laboratory (DE)
- European Molecular Biology Laboratory (DE)
Publication Details
- Journal
- Allergy
- Published
- 2025-11-06
- DOI
- https://doi.org/10.1111/all.70132
- Citations
- 1
- Primary Topic
- Monoclonal and Polyclonal Antibodies Research
- Type
- article
- Field-Weighted Citation Impact
- 1.36