The crystal structure of IgE Fc reveals an asymmetrically bent conformation.
The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the C epsilon 2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-A resolution has revealed these domains. The...
Hoofdauteurs: | Wan, T, Beavil, R, Fabiane, S, Beavil, A, Sohi, M, Keown, M, Young, R, Henry, A, Owens, R, Gould, H, Sutton, B |
---|---|
Formaat: | Journal article |
Taal: | English |
Gepubliceerd in: |
2002
|
Gelijkaardige items
-
Structural basis of the IgE-Fc epsilon RI interaction.
door: Beavil, A, et al.
Gepubliceerd in: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
door: Beavil, A, et al.
Gepubliceerd in: (1993) -
Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the Fc epsilon RI alpha chain.
door: Keown, M, et al.
Gepubliceerd in: (1995) -
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcIRI
door: Holdom, MD, et al.
Gepubliceerd in: (2011) -
The evolution of flexibility and function in the Fc domains of IgM, IgY, and IgE
door: Rosaleen A. Calvert, et al.
Gepubliceerd in: (2024-10-01)