1f2q
CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTORCRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR
Structural highlights
FunctionFCERA_HUMAN Binds to the Fc region of immunoglobulins epsilon. High affinity receptor. Responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The same receptor also induces the secretion of important lymphokines. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAllergic 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. Crystal structure of the human high-affinity IgE receptor.,Garman SC, Kinet JP, Jardetzky TS Cell. 1998 Dec 23;95(7):951-61. PMID:9875849[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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