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...
Những tác giả chính: | Holdom, MD, Davies, A, Nettleship, J, Bagby, S, Dhaliwal, B, Girardi, E, Hunt, J, Gould, H, Beavil, A, McDonnell, J, Owens, R, Sutton, B |
---|---|
Định dạng: | Journal article |
Ngôn ngữ: | English |
Được phát hành: |
2011
|
Những quyển sách tương tự
-
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
Bằng: Holdom, MD, et al.
Được phát hành: (2011) -
Structural basis of the IgE-Fc epsilon RI interaction.
Bằng: Beavil, A, et al.
Được phát hành: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
Bằng: Beavil, A, et al.
Được phát hành: (1993) -
The crystal structure of IgE Fc reveals an asymmetrically bent conformation.
Bằng: Wan, T, et al.
Được phát hành: (2002) -
Identification of contact residues in the IgE binding site of human FcεRIα
Bằng: Cook, J, et al.
Được phát hành: (1997)