| Autor: |
Wan, Tommy, Beavil, Rebecca L., Fabiane, Stella M., Beavil, Andrew J., Sohi, Maninder K., Keown, Maura, Young, Robert J., Henry, Alistair J., Owens, Ray J., Gould, Hannah J., Sutton, Brian J. |
| Předmět: |
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| Zdroj: |
Nature Immunology; Jul2002, Vol. 3 Issue 7, p681, 6p |
| Abstrakt: |
The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the Cε2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-Å resolution has revealed these domains. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the Cε3 and Cε4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving Cε2 must accompany binding to the mast cell receptor FcεRI.This may be the basis of the exceptionally slow dissociation rate of the IgE-FcεRI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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