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Crystal structure of sialylated IgG Fc: implications for the mechanism of intravenous immunoglobulin therapy.

Abstract:

Intravenous Ig consists of pooled human serum IgG and is widely used as an antiinflammatory agent. The fraction of IgG that is α2,6-sialylated exhibits anti-inflammatory activity and sialylation is proposed to enable binding to the cell surface lectin, dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN) (1). In a recent article in PNAS, Sondermann et al. propose a mechanism to explain the putative sialic acid-dependent binding of IgG Fc to DC-SIGN, as well...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted manuscript

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Publisher copy:
10.1073/pnas.1310657110

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Biology
Role:
Author
Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences of the United States of America Journal website
Volume:
110
Issue:
38
Pages:
E3544-E3546
Publication date:
2013-09-05
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
URN:
uuid:b220deb0-a83d-4c03-92a8-dff11386ad9e
Source identifiers:
418411
Local pid:
pubs:418411

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