Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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




Journal article


J Mol Biol

Publication Date





1061 - 1066


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