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...
| Main Authors: | , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2002
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| _version_ | 1797077789746135040 |
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| author | Wan, T Beavil, R Fabiane, S Beavil, A Sohi, M Keown, M Young, R Henry, A Owens, R Gould, H Sutton, B |
| author_facet | Wan, T Beavil, R Fabiane, S Beavil, A Sohi, M Keown, M Young, R Henry, A Owens, R Gould, H Sutton, B |
| author_sort | Wan, T |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T00:23:03Z |
| format | Journal article |
| id | oxford-uuid:7d32b32e-53b5-4f01-b88e-e76f5caea031 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:23:03Z |
| publishDate | 2002 |
| record_format | dspace |
| spelling | oxford-uuid:7d32b32e-53b5-4f01-b88e-e76f5caea0312022-03-26T21:02:00ZThe crystal structure of IgE Fc reveals an asymmetrically bent conformation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:7d32b32e-53b5-4f01-b88e-e76f5caea031EnglishSymplectic Elements at Oxford2002Wan, TBeavil, RFabiane, SBeavil, ASohi, MKeown, MYoung, RHenry, AOwens, RGould, HSutton, BThe 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. |
| spellingShingle | Wan, T Beavil, R Fabiane, S Beavil, A Sohi, M Keown, M Young, R Henry, A Owens, R Gould, H Sutton, B The crystal structure of IgE Fc reveals an asymmetrically bent conformation. |
| title | The crystal structure of IgE Fc reveals an asymmetrically bent conformation. |
| title_full | The crystal structure of IgE Fc reveals an asymmetrically bent conformation. |
| title_fullStr | The crystal structure of IgE Fc reveals an asymmetrically bent conformation. |
| title_full_unstemmed | The crystal structure of IgE Fc reveals an asymmetrically bent conformation. |
| title_short | The crystal structure of IgE Fc reveals an asymmetrically bent conformation. |
| title_sort | crystal structure of ige fc reveals an asymmetrically bent conformation |
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