Antibody

Antibodies are large glycoproteins that help protect the body against infection. They bind with a high degree of specificity to molecular structures (antigens) on infectious agents. This can lead to enhanced killing of microbes by phagocytes or complement.

They can be segregated into 5 classes of Immunoglobulin; IgG, IgM, IgE, IgA and IgD; their class is determi<span id="fck_dom_range_temp_1290335301683_70" /><span id="fck_dom_range_temp_1290335301683_641" />ned by the type of heavy chain in the antibody. Each of them has different distribution in the body. IgM and IgA are multimeric. The other three are monomeric antibodies. IgA exist as both multimeric and monomeric antibody in different tissues of the body.   The classes differ in their structure and function.

Structure

Antibody molecules are in the shape of a Y, and all consist of three parts that are connected together by disulphide bonds in order to form this Y shape. Antibodies are also made up of a two polypeptide chains; a heavy chain and a light chain. All immunoglobulin molecules contain heavy and light chains that are identical, giving rise to two identical antigen-binding sites.  The stem of the Y is a constant region composed of only heavy chains.  The ends of the arms of the Y form variable regions composed of heavy and light chains.  The constant regions can be used to distinguish between the 5 classes of immunoglobulins while the variable regions 'vary' between different antibody molecules.

Antibody domains

Through amino acid sequence analysis, homology regions were found which are referred to as 'homology domains'.  The L chain comprises 2 domains and the H chain can have either 4 or 5 domains.  Each domain is around 110 amino acids in length, comprised of two beta sheets, linked by a disulphide bridge.  It is worth noting dmoains are also paired - folded units within the protein,

 

Antigen-binding sites bind to epitopes on the antigen. The epitope can be linear (continuous) or conformational (discontinuous)