What is the basic structure of antibodies?
The basic structure of the antibody is a protein molecule in the shape of a Y with two heavy and two light polypeptide chains. One can visualize the structure of antibodies falling as in standing on the lower letter L with a line on both outer edges and parallel to V. Lower L, known as the FC antibodies, includes two heavy polypeptide chains that rise upwards to form a V or FAB area. The inner lines in the end of heavy chains, while the outer lines are light polypeptide chains.
antibody or immunoglobulin is a protein produced by plasma cells in the body. The body's immune system uses antibodies to recognize antigens found in enemy foreign objects such as bacteria and viruses, and get rid of them. Each antibody is produced in response to a specific antigen found on foreign attackers. These binding sites are an area of the largest variations between any two types of antibodies. This is because the antibody uses the ligamentBile places to connect to an antigen that has been designed to focus.
The ends of the light chains can be classified as Kappa or Lambda in mammals, while the lower vertebrates also have a form of IOTA. Make-up of a heavy chain determines the subclass of antibodies. These heavy chains may vary in size and composition. Some are composed of approximately 450 amino acids, while others have around 550.
The tip of each type of antibody consists of about 110 to 130 amino acids. These tips are divided into two regions. Hypervariable (HV) area contains the widest variations in amino acids, while the frame (FR) area is constant and stable. The HV area will establish direct contact with the antigen. Therefore, it is sometimes referred to as free determining area (CDR).
While the upper end of the antibody structure is bound to the antigen, the FC area, also known as the fragment of the crystallizable area, determines how againstThe substance deals with antigen. This means that the antibody can regulate and stimulate a suitable immune response. Constant areas can be divided into five isotype classes: immunoglobulin M (IgM), immunoglobulin G (IgG), immunoglobulin E (IgE), immunoglobulin D (IgD) and immunoglobulin and (IgA). The composition of the constant area of each isotype is identical.