Crystal structure of the human high-affinity IgE receptor.
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Garman SC, Kinet JP, Jardetzky TS
Crystal structure of the human high-affinity IgE receptor.
Cell. 1998 Dec 23;95(7):951-61.
- PubMed ID
- 9875849 [ View in PubMed]
- Abstract
Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolution. The structure reveals a highly bent arrangement of immunoglobulin domains that form an extended convex surface of interaction with IgE. A prominent loop that confers specificity for IgE molecules extends from the receptor surface near an unusual arrangement of four exposed tryptophans. The crystal structure of the IgE receptor provides a foundation for the development of new therapeutic approaches to allergy treatment.