 On average, the number of amino acid residues for each domain can be

taken as 110.
Structure of IgG

1. IgG antibodies are large globular proteins with a molecular weight of about
150 kDa made of four peptide chains.
2. It contains two identical γ (gamma) heavy chains of about 50 kDa and two
identical light chains of about 25 kDa, thus a tetrameric quaternary
structure.
3. The two heavy chains are linked to each other and to a light chain each
by disulfide bonds. The resulting tetramer has two identical halves, which
together form the Y-like shape.
4. Each end of the fork contains an identical antigen binding site.
5. The Fc regions of IgGs bear a highly conserved N-glycosylation site at
asparagine 297 in the constant region of the heavy chain.
6. The N-glycans are present attached to the heavy chain.
7. The N-glycan composition in IgG has been linked to several autoimmune,
infectious and metabolic diseases

IgG is the main type of antibody found in blood and extracellular fluid, allowing it
to control infection of body tissues. By binding many kinds of pathogens such
as viruses, bacteria, and fungi, IgG protects the body from infection.
Functions of IgG

 IgG-mediated binding of pathogens causes their immobilization and binding

together via agglutination; IgG coating of pathogen surfaces (known
as opsonization) allows their recognition and ingestion by phagocytic immune
cells leading to the elimination of the pathogen itself
 IgG activates all the classical pathway of the complement system, a cascade of
immune protein production that results in pathogen elimination
 IgG also binds and neutralizes toxins
 IgG also plays an important role in antibody-dependent cell-mediated
cytotoxicity (ADCC) and intracellular antibody-mediated proteolysis
 IgG is also associated with type II and type III hypersensitivity reactions.