Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions.
Crispin M., Bowden TA., Coles CH., Harlos K., Aricescu AR., Harvey DJ., Stuart DI., Jones EY.
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.