When the amino acid sequence of antibody molecules that bind to different epitopes are compared, tremendous variation is seen in the domains that form the ends of the Fab regions. These domains make up the variable regions of the antibody molecule; they contain the antigen-binding sites. The differences provided by the variable regions account for the specificity of antibody molecules.
Each antibody binds via the antigen-binding site to the antigen that induced its production. The interaction depends on close complementarities between the antigen-binding site and the specific antigenic epitope. The fit must be precise, because the bonds that hold the antibody and antigen are non-covalent, weak, and have short range. Although the forces holding the antigen and antibody together are weak, many such bonds are formed, usually keeping the two together very effectively. Nevertheless, the antigen-antibody interaction is reversible. Upon reversal, both antigen and antibody are unchanged.
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