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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.

Original publication

DOI

10.1016/j.jmb.2009.02.033

Type

Journal article

Journal

J Mol Biol

Publication Date

17/04/2009

Volume

387

Pages

1061 - 1066

Keywords

Antibody-Dependent Cell Cytotoxicity, Carbohydrate Sequence, Crystallography, X-Ray, Glycosylation, Humans, Immunoglobulin Fc Fragments, Immunoglobulin G, In Vitro Techniques, Models, Molecular, Oligosaccharides, Protein Structure, Tertiary, Recombinant Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Static Electricity