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Journal article

Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the Fc epsilon RI alpha chain.

Abstract:

The interaction between immunoglobulin E (IgE) and its high-affinity receptor Fc epsilon RI is central to allergic disease. The binding site for Fc epsilon RI lies in the third constant region domain of the epsilon heavy chain of IgE (C epsilon 3). Identical epitopes on the two C epsilon 3 domains in the IgE-Fc are predicted to be on opposite sides of the structure, and therefore each could bind independently to a receptor molecule. Titrations, however, reveal that the IgE-Fc forms an equimol...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.92.6.1841

Authors


Ghirlando, R More by this author
Beavil, AJ More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
92
Issue:
6
Pages:
1841-1845
Publication date:
1995-03-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:16012ec2-15b0-467a-947f-71559b188ee2
Source identifiers:
171610
Local pid:
pubs:171610

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