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Journal article

Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.

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...

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Publication status:
Published

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Publisher copy:
10.1038/nsmb.2044

Authors


Holdom, MD More by this author
Davies, AM More by this author
Nettleship, JE More by this author
Dhaliwal, B More by this author
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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

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