Biomolecular NMR Assignments · 2014 · 51 citations · 18 references
Life SciencesBiochemistryImmunologyAntibody EngineeringGlycobiologyStructural BiologyAntibody CharacterizationAntibody StructureGlycan-protein InteractionsGlycoengineering Of AntibodiesN-linked GlycosylationProtein GlycosylationAntibodiesAntibody Glycosylation EffectsChimeric Antibody ProductionChinese Hamster Ovary CellsFc Region StructureImmunoglobulin GlycosylationMolecular Conformational DynamicsProtein Glycosylation Analysis
The Fc portion of immunoglobulin G (IgG) recruits complements and its cognate receptors, thereby promoting defensive mechanisms in the humoral immune system. These effector functions critically depend on N-glycosylation at the Fc region, which is therefore regarded as a crucial factor in the design and production of therapeutic antibodies. NMR spectroscopy plays a unique role in the characterization of conformational dynamics and intermolecular interactions of IgG-Fc in solutions. Here, we report NMR assignments of the glycosylated Fc fragment (Mr 53 kDa), cleaved from a chimeric antibody with human IgG1 constant regions, which was produced in Chinese hamster ovary cells with uniform (13)C- and (15)N-labeling.
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