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Domains of the immunoglobulin

Apr 9th 2015 at 8:24 PM


Domains of the immunoglobulin

The Ig monomer is a "Y"-shaped molecule(antibody technology). It has four polypeptide chains - two identical ''heavy chains'' and two identical ''light chains''. There are five types of mammalian Ig heavy chain denoted by the Greek letters: α, δ, ε, γ, and μ. These form respectively IgA, IgD, IgE, IgG and IgM.

The Ig has a paratope at the amino terminal end of the antibody monomer. This exists at the variable domains from the heavy and light chains. The variable domain is the FV region and is the most important region for binding to antigens. At this region are variable loops of β-strands. On the light chain are three loops - VL and on the heavy chain are three loops VH. These are responsible for binding to the antigen. These loops are referred to as the complementarity determining regions (CDRs). These CDRs are also called idiotypes.

The base of the Y modulates the immune cell activity. This region is called the ''Fc (Fragment, crystallizable) region''. In this area are two heavy chains that contribute two or three constant domains depending on the class of the antibody(antibody production).

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