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Antibody Structure

Antibodies are heavy (~150 kDa) globular plasma proteins. They have sugar chains added to some of their amino acid residues. In other words, antibodies are ''glycoproteins''. 

The basic functional unit of each antibody is an immunoglobulin (Ig) monomer (containing only one Ig unit); secreted antibodies can also be dimeric with two Ig units as with IgA, tetrameric with four Ig units like teleost fish IgM, or pentameric with five Ig units, like mammalian IgM.

Immunoglobulin domains

The Ig monomer is a "Y"-shaped molecule that consists of four polypeptide chains; two identical ''heavy chains'' and two identical ''light chains'' connected by disulfide bonds. 

They have a characteristic immunoglobulin fold in which two beta sheets create a “sandwich” shape, held together by interactions between conserved cysteines and other charged amino acids.

Heavy chain

There are five types of mammalian Ig heavy chain denoted by the Greek letters: α, δ, ε, γ, and μ.

The paratope is shaped at the amino terminal end of the antibody monomer by the variable domains from the heavy and light chains. The variable domain is also referred to as the FV region and is the most important region for binding to antigens. 

More specifically, variable loops of β-strands, three each on the light (VL) and heavy (VH) chains are responsible for binding to the antigen. These loops are referred to as the complementarity determining regions (CDRs).

In the framework of the immune network theory, CDRs are also called idiotypes. According to immune network theory, the adaptive immune system is regulated by interactions between idiotypes.

The base of the Y plays a role in modulating immune cell activity. This region is called the ''Fc (Fragment, crystallizable) region'', and is composed of two heavy chains that contribute two or three constant domains depending on the class of the antibody.

Further Reading


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