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...
المؤلفون الرئيسيون: | 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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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2011
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مواد مشابهة
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Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
حسب: Holdom, MD, وآخرون
منشور في: (2011) -
Structural basis of the IgE-Fc epsilon RI interaction.
حسب: Beavil, A, وآخرون
منشور في: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
حسب: Beavil, A, وآخرون
منشور في: (1993) -
The crystal structure of IgE Fc reveals an asymmetrically bent conformation.
حسب: Wan, T, وآخرون
منشور في: (2002) -
Identification of contact residues in the IgE binding site of human FcεRIα
حسب: Cook, J, وآخرون
منشور في: (1997)