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...
المؤلفون الرئيسيون: | Wan, T, Beavil, R, Fabiane, S, Beavil, A, Sohi, M, Keown, M, Young, R, Henry, A, Owens, R, Gould, H, Sutton, B |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2002
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مواد مشابهة
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Structural basis of the IgE-Fc epsilon RI interaction.
حسب: Beavil, A, وآخرون
منشور في: (1993) -
Structural basis of the IgE-Fc epsilon RI interaction.
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منشور في: (1993) -
Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the Fc epsilon RI alpha chain.
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Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcIRI
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The evolution of flexibility and function in the Fc domains of IgM, IgY, and IgE
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منشور في: (2024-10-01)