The crystal structure of IgE Fc reveals an asymmetrically bent conformation |
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Authors: | 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 |
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Institution: | The Randall Centre, King's College London, New Hunt's House, London SE1 1UL, UK. |
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Abstract: | 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. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving C epsilon 2 must accompany binding to the mast cell receptor Fc epsilon RI. This may be the basis of the exceptionally slow dissociation rate of the IgE-Fc epsilon RI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells. |
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