Antibody | Structure | Illustration | Graphics | Design | Basic Science Series

Antibody | Structure | Illustration | Graphics | Design | Basic Science Series

antibody, immunoglobulin, B cells, immune system, foreign substances, viruses, bacteria, pathogens, defending, antigen, polypeptide chains, heavy chains, light chains, disulfide bonds, variable region, constant region, isotype, IgG, IgM, IgA, IgE, IgD, hypervariable regions, complementarity-determining regions (CDRs), paratope, epitope, effector functions, complement fixation, antibody-dependent cellular cytotoxicity, opsonization, monomers, dimers, pentamers, activate complement, cross placenta.

An antibody (also known as immunoglobulin) is a protein molecule produced by B cells of the immune system in response to the presence of foreign substances, such as viruses, bacteria, and other pathogens. Antibodies play a critical role in defending the body against infection by binding to specific antigens on the surface of these pathogens and marking them for destruction by other immune cells.

The basic structure of an antibody molecule consists of four polypeptide chains, two heavy chains, and two light chains, linked together by disulfide bonds. Each chain has a variable region and a constant region.

The variable regions of the heavy and light chains form the antigen-binding site, which is specific for a particular antigen. The constant regions of the heavy chains determine the antibody's class or isotype, such as IgG, IgM, IgA, IgE, or IgD, which have different functions in the immune system.

The amino acid sequence of the variable region of the antibody chain determines its specificity for a particular antigen. The variable region contains hypervariable regions, also known as complementarity-determining regions (CDRs), which directly interact with the antigen. The arrangement of these hypervariable regions forms a three-dimensional structure, called the paratope, which matches the three-dimensional structure of the antigen's epitope.

The constant region of the heavy chain determines the antibody's effector functions, such as complement fixation, antibody-dependent cellular cytotoxicity, and opsonization. The constant region of the light chain is responsible for pairing with the heavy chain and does not have any known effector functions.

Antibodies can exist in different forms, such as monomers, dimers, or pentamers, depending on their isotype. For example, IgG antibodies are monomers, while IgM antibodies are pentamers. The different forms of antibodies have different properties, such as their ability to activate complement or cross the placenta.

In summary, the detailed structure of an antibody consists of four polypeptide chains, two heavy chains, and two light chains, with variable regions that form the antigen-binding site and constant regions that determine the antibody's class and effector functions.

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