Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 387, Issue 5, Pages 1061-1066Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.02.033
Keywords
antibody; glycosylation; oligomannose; antibody engineering; kifunensine
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Funding
- Cancer Research UK
- UK Medical Research Council
- European Commission as SPINE2 Complexes [FP6-RTD-031220]
- Wellcome Trust
- MRC [G0700232, G0500365, G9900061, G0500367] Funding Source: UKRI
- Medical Research Council [G0500365, G0700232, G9900061, G0500367] Funding Source: researchfish
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Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding. (C) 2009 Elsevier Ltd. All rights reserved.
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