1f2q | pdb_00001f2q
CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR
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| 1f2q, resolution 2.40Å | |||||||||||||
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| Ligands: | MAN, NAG | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1F2Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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