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The crystal structure of CHIR-AB1: a primordial avian classical Fc receptor.

Abstract:

CHIR-AB1 is a newly identified avian immunoglobulin (Ig) receptor that includes both activating and inhibitory motifs and was therefore classified as a potentially bifunctional receptor. Recently, CHIR-AB1 was shown to bind the Fc region of chicken IgY and to induce calcium mobilization via association with the common gamma-chain, a subunit that transmits signals upon ligation of many different immunoreceptors. Here we describe the 1.8-A-resolution crystal structure of the CHIR-AB1 ectodomain...

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Publisher copy:
10.1016/j.jmb.2008.06.082

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Kaiser, JT More by this author
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Journal:
Journal of molecular biology
Volume:
381
Issue:
4
Pages:
1012-1024
Publication date:
2008-09-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:7193d359-09cb-4f44-a9ce-256fe4f781e2
Source identifiers:
482810
Local pid:
pubs:482810

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