The flexibility of antibody molecules principally derives from the str
ucture of the hinge region. It has generally been accepted that the fl
exibility of the IgG hinge is necessary for complement activation to o
ccur; however, recent studies dispute this premise. As described here
by Ole Henrik Brekke, Terje Michaelsen and Inger Sandlie, it now appea
rs that the only requirement of the hinge region for complement activa
tion is the presence of inter-heavy-chain disulfide bonds(s). Furtherm
ore, the structural basis for the differences between IgG subclasses w
ith respect to effector functions appear to be located within the C(H)
2 domain of the immunoglobulin molecule.