What Is the Structural Composition of the Fc Region of IgG Antibody
The Fc region of the IgG antibody refers to the constant region at the carboxyl-terminal end of the antibody molecule, which bears carbohydrate moieties and is primarily formed by the constant regions of two associated heavy chains. This region comprises two main domains, CH2 and CH3, connected by a flexible hinge region. The hinge, enriched in cysteine residues, confers structural flexibility that facilitates effective engagement with Fc receptors.
The CH2 domain contains one or more attached oligosaccharide chains, which are critical for maintaining IgG stability and modulating its binding affinity to Fc receptors. The glycan composition within this domain can influence various effector functions of IgG, including pro-inflammatory signaling and antibody-dependent cell-mediated cytotoxicity (ADCC).
The CH3 domain is primarily responsible for mediating the oligomerization of IgG molecules and facilitating interactions with Fc receptors located on the surface of immune cells such as macrophages, dendritic cells, and natural killer cells. These receptor-ligand interactions potentiate immune cell functions, including phagocytosis and ADCC, thereby contributing to the antibody’s overall effector activity.
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