Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcεRI
Published in Nature Structural & Molecular Biology, 2011
Recommended citation: MD Holdom, AM Davies, JE Nettleship, SC Bagby, B Dhaliwal, E Girardi, J Hunt, HJ Gould, AJ Beavil, JM McDonnell, RJ Owens, and BJ Sutton (2011). "Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcεRI." Nature Struct Mol Biol 18:571.
Entropy drives the high-affinity receptor interaction underlying asthma and allergy. X-ray crystallography, surface plasmon resonance, thermodynamics.