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• W2030379652 endingPage "359" @default.
• W2030379652 startingPage "346" @default.
• W2030379652 abstract "Immunoglobulin G (IgG) glycoproteins are used as therapeutic antibodies, and the biopharmaceutical properties and efficacies of IgG-based drugs are determined by their N-glycosylation. A pair of N-glycans in the Fc portion of IgG exhibit microheterogeneities depending on the physiological and pathological conditions of individuals and the expression method used in biopharmaceutical applications. The glycoforms of Fc critically affect its quaternary conformation and effector functions promoted via interactions with Fcγ receptors (FcγRs) and complement component C1q. This is exemplified by the drastic enhancement of antibody-dependent cell-mediated cytotoxicity (ADCC) on defucosylation of IgG-Fc N-glycans. Accumulating crystal structures have provided the structural basis of human IgG1-Fc and a panel of FcγRs. In particular, crystallographic data demonstrate that the complex formation between non-fucosylated IgG1-Fc and FcγRIIIa is reinforced by interactions of N-glycans of these two glycoproteins. Recent computational approaches have successfully visualized the dynamic behaviors of IgG molecules, focusing on the IgG1-Fc glycoproteins and their complexes with FcγRIIIa in solution. Molecular dynamic simulations of Fc indicated that the core fucosylation of N-glycans restricts the conformational freedom of the proximal tyrosine residue of functional importance, thereby precluding its interaction with FcγRIIIa. Moreover, the Fc N-glycans restrict the domain motions and endow structural plasticity and integrity through dynamic intramolecular interaction networks in the molecule. These structural and dynamic views of IgG-Fc as a glycoprotein not only explain the mechanisms behind the N-glycan-dependent effector functions but also provide useful insights for designing therapeutic antibodies with improved functionality by controlling their conformational dynamics and subsequent interactions." @default.
• W2030379652 created "2016-06-24" @default.
• W2030379652 creator A5047494990 @default.
• W2030379652 creator A5052716791 @default.
• W2030379652 creator A5053746071 @default.
• W2030379652 date "2010-05-01" @default.
• W2030379652 modified "2023-10-16" @default.
• W2030379652 title "Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system" @default.
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