1f2q
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(New page: 200px<br /> <applet load="1f2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2q, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:42, 12 November 2007
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CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR
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 with NAG as ligand. 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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