1. Crystal structure of the human high-affinity IgE receptor.
- Author
-
Garman SC, Kinet JP, and Jardetzky TS
- Subjects
- Amino Acid Sequence, Animals, Binding Sites, Cell Line, Crystallization, Crystallography, X-Ray methods, Glycosylation, Humans, Immunoglobulin E metabolism, Models, Molecular, Molecular Sequence Data, Molecular Weight, Protein Conformation, Protein Structure, Tertiary, Receptors, IgE genetics, Receptors, IgE isolation & purification, Receptors, IgE metabolism, Recombinant Proteins chemistry, Sequence Alignment, Solubility, Tryptophan, Receptors, IgE chemistry
- 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.
- Published
- 1998
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