Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcɛRI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-Å-resolution crystal structure of human I...
Autors principals: | Holdom, MD, Davies, A, Nettleship, J, Bagby, S, Dhaliwal, B, Girardi, E, Hunt, J, Gould, H, Beavil, A, McDonnell, J, Owens, R, Sutton, B |
---|---|
Format: | Journal article |
Idioma: | English |
Publicat: |
2011
|
Ítems similars
-
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcIRI
per: Holdom, MD, et al.
Publicat: (2011) -
FceRI density and spontaneous secretion from human basophils.
per: Donald MacGlashan
Publicat: (2017-01-01) -
A spatio-temporal model reveals self-limiting FcɛRI cross-linking by multivalent antigens
per: Md Shahinuzzaman, et al.
Publicat: (2018-01-01) -
A TNFRSF14-FcɛRI-mast cell pathway contributes to development of multiple features of asthma pathology in mice
per: Riccardo Sibilano, et al.
Publicat: (2016-12-01) -
Structural basis of the IgE-Fc epsilon RI interaction.
per: Beavil, A, et al.
Publicat: (1993)