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pubmed-article:2523358pubmed:abstractTextStructural interactions between IgE and its high-affinity receptor have been investigated with the methods of fluorescence resonance energy transfer and genetic engineering. The results indicate that IgE has a bent conformation when bound to receptor on the cell surface and that the site of interaction is contained in the C epsilon 2 and C epsilon 3 domains; the C-terminal domain, C epsilon 4, is not required for binding. Cross-linking of IgE-receptor complexes is required for signal transduction across the plasma membrane. Binding studies with defined bivalent ligands indicate that structural and/or kinetic features determine the functional effectiveness of the cross-linked states.lld:pubmed
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pubmed-article:2523358pubmed:articleTitleInteraction of IgE with its high-affinity receptor. Structural basis and requirements for effective cross-linking.lld:pubmed
pubmed-article:2523358pubmed:affiliationDepartment of Chemistry, Baker Laboratory, Cornell University, Ithaca, N.Y.lld:pubmed
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