Antibodies are the proteins produced by the B-lymphocytes in response to the antigen or foreign bodies.
- They are also known as immunoglobulins (Ig).
- They are found in the serum fraction of the blood and produced by plasma cells. Approximately 20% of the plasma protein is immunoglobulins.
- Antibodies can travel throughout the body to find and bind to their target antigens (foreign substances).
- The molecular weight of antibodies are generally ranges between 150000-900000 Da.
Structure of Antibody
IgG is the most studied immunoglobulin and serves as a model of the basic structural unit of all antibodies.
The molecule of IgG is Y-shaped and consists of 4-polypeptide chains; two identical heavy (H) chains and two identical light (L) chains which are connected by a disulfide bond.
Different parts of an antibody molecule are described below:
Heavy and Light Chains
- There are 4 peptide chains in an antibody molecule.
- Two long chains called heavy chains and two long chains called light chains.
- Each heavy chain contains more than 400 amino acids, while the light chain usually has 200 amino acids.
- In mammals, H chains are α, δ, ε, γ, and μ types, but L chains are two types known as lambda (λ) and kappa (κ).
Disulfide Bonds and Hinge Region
- Each light chain is linked to a heavy chain by a disulfide bond.
- There are also two disulfide bonds connecting the two heavy chains.
- This part of the antibody is called the hinge region, which functions in maintaining the flexibility of the antibody. Here, the arms of the antibody can bend and form a Y-shaped structure.
- There are also intrachain disulfide bonds in both light and heavy chains.
Constant and Variable Regions
- Intrachain disulfide bonds form loops.
- Each loop is called a domain.
- The light chain contains a single variable domain (VL)and a single constant domain (CL), while the heavy chain contains a single variable domain (VH) and three or four constant domains (CH).
- Constant domains from the constant region and variable domains form the variable region in each of the heavy and light chains.
Fragment Antigen Binding (Fab) and Fragment Crystalizable (Fc)
- Two identical fragments of the Y-shaped structure of the antibody molecule function for antigen binding sites. This is known as the fragment antigen binding (Fab).
- The antigen binding sites bind to specific antigens in a lock and key pattern and form an antigen-antibody complex.
- The tail section of the antibody is incapable of binding antigen and can be crystallized. This is called fragment crystallizable (Fc).