Abstract
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 language | English |
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Pages (from-to) | 1061-6 |
Number of pages | 6 |
Journal | Journal of Molecular Biology |
Volume | 387 |
Issue number | 5 |
DOIs | |
Publication status | Published - 17 Apr 2009 |
Keywords / Materials (for Non-textual outputs)
- Antibody-Dependent Cell Cytotoxicity
- Carbohydrate Sequence
- Crystallography, X-Ray
- Glycosylation
- Humans
- Immunoglobulin Fc Fragments
- Immunoglobulin G
- Models, Molecular
- Oligosaccharides
- Protein Structure, Tertiary
- Recombinant Proteins
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Static Electricity