Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcIRI
Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcI RI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-Ã.-resolution crystal structure of human...
Main Authors: | Holdom, MD, Davies, A, Nettleship, J, Bagby, S, Dhaliwal, B, Girardi, E, Hunt, J, Gould, H, Beavil, A, McDonnell, J, Owens, R, Sutton, B |
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פורמט: | Journal article |
שפה: | English |
יצא לאור: |
2011
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פריטים דומים
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Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
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The crystal structure of IgE Fc reveals an asymmetrically bent conformation.
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