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...
Κύριοι συγγραφείς: | 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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Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
2011
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Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
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Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
ανά: Holdom, MD, κ.ά.
Έκδοση: (2011) -
Structural basis of the IgE-Fc epsilon RI interaction.
ανά: Beavil, A, κ.ά.
Έκδοση: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
ανά: Beavil, A, κ.ά.
Έκδοση: (1993) -
The crystal structure of IgE Fc reveals an asymmetrically bent conformation.
ανά: Wan, T, κ.ά.
Έκδοση: (2002) -
Identification of contact residues in the IgE binding site of human FcεRIα
ανά: Cook, J, κ.ά.
Έκδοση: (1997)