Structure of Antibody Explain in brief.
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Antibodies, also known as immunoglobulins (Ig), are Y-shaped proteins that are produced by B cells in response to the presence of a foreign substance, known as an antigen. Each antibody molecule is composed of four polypeptide chains, two identical heavy chains, and two identical light chains, which are linked together by disulfide bonds.
The basic structure of an antibody molecule consists of two identical antigen-binding fragments (Fab) and a single crystallizable fragment (Fc). The Fab region is located at the tips of the Y-shaped molecule and is responsible for binding to specific antigens. The Fc region is located at the base of the Y and is responsible for the effector functions of the antibody, such as activating complement and binding to Fc receptors on immune cells.
Each Fab region contains a variable region and a constant region. The variable region is responsible for binding to the antigen and is highly variable between different antibodies, while the constant region is more conserved and is responsible for the structure and function of the antibody molecule.
The heavy and light chains each consist of a variable region and a constant region. The variable regions of the heavy and light chains combine to form the antigen-binding site of the Fab region, while the constant regions of the heavy chains form the Fc region.
Overall, the structure of an antibody molecule allows it to specifically recognize and bind to a wide variety of antigens, and to elicit a range of effector functions to help eliminate the antigen from the body.
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