A fluorescent biosensor reveals conformational changes in human immunoglobulin E Fc: Implications for mechanisms of receptor binding, inhibition, and allergen recognition

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A fluorescent biosensor reveals conformational changes in human immunoglobulin E Fc: Implications for mechanisms of receptor binding, inhibition, and allergen recognition

IgE binding to its high affinity receptor Fc?RI on mast cells and basophils is a key step in the mechanism of allergic disease and a target for therapeutic intervention. Early indications that IgE adopts a bent structure in solution have been confirmed by recent x-ray crystallographic studies of IgE...

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Bibliographic Details
Main Authors:	Hunt, J., Keeble, A., Dale, R., Corbett, Melissa, Beavil, R., Levitt, J., Swann, M., Suhling, K., Ameer-Beg, S., Sutton, B., Beavil, A.
Format:	Journal Article
Published:	American Society for Biochemistry and Molecular Biology, Inc. 2012
Subjects:	FRET Biosensor Biosensors Antibodies IgE Immunology CD23 Fluorescence Resonance Energy Transfer (FRET) Omalizumab Protein Conformation Biophysics
Online Access:	http://www.jbc.org/content/287/21/17459.full.pdf+html?sid=79302ac6-c192-4b51-abe8-4ffd1d5a5a87 http://hdl.handle.net/20.500.11937/21883

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