Abstract
IgE antibodies play a central role in allergic disease. They recognize allergens via their Fab regions, whilst their effector functions are controlled through interactions of the Fc region with two principal cell surface receptors, Fc epsilon RI and CD23. Crosslinking of Fc epsilon RI-bound IgE on mast cells and basophils by allergen initiates an immediate inflammatory response, while the interaction of IgE with CD23 on B-cells regulates IgE production. We have determined the structures of the C-type lectin "head" domain of CD23 from seven crystal forms. The thirty-five independent structures reveal extensive conformational plasticity in two loops that are critical for IgE binding.
Original language | English |
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Article number | N/A |
Pages (from-to) | 693-697 |
Number of pages | 5 |
Journal | Molecular Immunology |
Volume | 56 |
Issue number | 4 |
DOIs | |
Publication status | Published - 31 Dec 2013 |
Keywords
- Allergy
- Immunoglobulin E
- Antibody-receptor interactions
- Immunology
- X-ray crystallography
- FC-EPSILON-RI
- LOW-AFFINITY RECEPTOR
- MACROMOLECULAR CRYSTALLOGRAPHY
- IMMUNOGLOBULIN-E
- DOMAIN
- REFINEMENT
- FRAGMENT
- INHIBITION
- SOFTWARE
- BUSTER