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Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis

Abstract:

Human IgG Fc glycosylation modulates immunological effector functions such as antibody-dependent cellular cytotoxicity and phagocytosis. Engineering of Fc glycans therefore enables fine-tuning of the therapeutic properties of monoclonal antibodies. The N-linked glycans of Fc are typically complex-type, forming a network of noncovalent interactions along the protein surface of the Cγ2 domain. Here, we manipulate the mammalian glycan-processing pathway to trap IgG1 Fc at sequential stages of ma...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1021/ja306068g

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Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Biology
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Biology
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, Biochemistry
Role:
Author
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Funding agency for:
Aricescu, AR
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Funding agency for:
Jones, EY
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Publisher:
American Chemical Society Publisher's website
Journal:
Journal of the American Chemical Society Journal website
Volume:
134
Issue:
42
Pages:
17554-17563
Publication date:
2012-10-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:4f06077c-53dd-4e36-b0bf-9be13bba144c
Source identifiers:
353920
Local pid:
pubs:353920

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