Each of the four chain has a variable(V) region at its amino terminus, which contributes to the antigen-binding site, and a constant (C) region, which determines the isotype. The isotype of the heavy chain determines the functional properties of antibody. The light chain are bound to the heavy chains by many noncovalent interactions and by disulfide bonds, and the V regions of the heavy and light chain pair in each arm ot the Y to generate two identical antigen-binding sites, which lie at the tips of the arms of the Y. The possession of two antigen-binding sites allows antibody molecles to cross-link antigens and to bind them much more stably and with higher avidity. The trunk of the Y, called the Fc fragment, is composed of the carboxy-terminal domains of the heavy chain. Joining the arms of the Y to the trunk are the flexible hinge regions. The Fc fragment and hinge regions differ in antibodies of different isotypes, thus determining their functional properties. However, the overall organization of the domains is similar in all isotypes.