Ms.
Arti Soni
Kanoria PG Mahila Mahavidyalaya, Jaipur
Structure of antibody
1 Basic Structure:
- Composed of four polypeptide chains: two identical heavy chains and two identical light
chains.
- Chains are connected by disulfide bonds, forming a Y-shaped molecule.
2 Regions:
- Variable Region (Fab):
- Located at the tips of the Y.
- Responsible for antigen binding.
- High variability to recognize a wide range of antigens.
- Constant Region (Fc):
- Forms the stem of the Y.
- Determines the antibody's class (isotype).
- Mediates effector functions by binding to cell receptors and complement proteins.
3 Chains:
- Heavy Chains:
- Larger polypeptides (~50 kDa each).
- Types: α (IgA), δ (IgD), ε (IgE), γ (IgG), and μ (IgM).
- Light Chains:
- Smaller polypeptides (~25 kDa each).
- Types: κ (kappa) and λ (lambda).
4 Domains:
- Each chain consists of multiple immunoglobulin domains.
- Heavy chains have one variable domain (VH) and three to four constant domains (CH1, CH2,
CH3, and sometimes CH4).
- Light chains have one variable domain (VL) and one constant domain (CL).
5 Functional Sites:
- Antigen-Binding Sites:
- Located in the variable regions of both heavy and light chains.
- Each antibody has two identical antigen-binding sites.
- Effector Function Sites:
- Located in the Fc region.
- Involved in interactions with immune cells and complement system.
