- Abstract:
-
Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcɛRI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-Å-resolution crystal structure of human IgE-Fc (consisting of the Cɛ2, Cɛ3 and Cɛ4 domains) bound to the extracellular domains of the FcɛRI α chain. Comparison with the structure of free IgE-Fc (reported here at a resolution of 1.9 Å) sho...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1038/nsmb.2044
-
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- Journal:
- Nature structural and molecular biology
- Volume:
- 18
- Issue:
- 5
- Pages:
- 571-576
- Publication date:
- 2011-05-05
- DOI:
- EISSN:
-
1545-9985
- ISSN:
-
1545-9993
- URN:
-
uuid:07ce34ff-9c5b-4cf7-91cd-138f7a33e82c
- Source identifiers:
-
139122
- Local pid:
- pubs:139122
- Copyright date:
- 2011
Journal article
Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.
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