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

Abstract:

Among antibody classes, IgE has a uniquely slow dissociation rate from, and high affinity for, its cell surface receptor FcI RI. We show the structural basis for these key determinants of the ability of IgE to mediate allergic hypersensitivity through the 3.4-Ã.-resolution crystal structure of human IgE-Fc (consisting of the CI 2, CI 3 and CI 4 domains) bound to the extracellular domains of the FcI RI Î ± chain. Comparison with the structure of free IgE-Fc (reported here at a resolution of 1....

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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:f6b07b5e-04e5-43c8-a312-78b5aa7a6d54
Source identifiers:
149832
Local pid:
pubs:149832
Language:
English

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