Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions.

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 cellul...

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Бібліографічні деталі
Автори: Crispin, M, Bowden, T, Coles, C, Harlos, K, Aricescu, A, Harvey, D, Stuart, D, Jones, E
Формат: Journal article
Мова:English
Опубліковано: 2009
Опис
Резюме: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.