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...
Үндсэн зохиолчид: | Holdom, MD, Davies, A, Nettleship, J, Bagby, S, Dhaliwal, B, Girardi, E, Hunt, J, Gould, H, Beavil, A, McDonnell, J, Owens, R, Sutton, B |
---|---|
Формат: | Journal article |
Хэл сонгох: | English |
Хэвлэсэн: |
2011
|
Ижил төстэй зүйлс
Ижил төстэй зүйлс
-
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
-н: Holdom, MD, зэрэг
Хэвлэсэн: (2011) -
Structural basis of the IgE-Fc epsilon RI interaction.
-н: Beavil, A, зэрэг
Хэвлэсэн: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
-н: Beavil, A, зэрэг
Хэвлэсэн: (1993) -
The crystal structure of IgE Fc reveals an asymmetrically bent conformation.
-н: Wan, T, зэрэг
Хэвлэсэн: (2002) -
Identification of contact residues in the IgE binding site of human FcεRIα
-н: Cook, J, зэрэг
Хэвлэсэн: (1997)