Abstract
Prior to the advent of high-resolution x-ray diffraction, the work of many chemists and physical chemists had led to a “low-resolution” picture of the antibody molecule that is summarized in Fig. 1 (Edelman and Gall, 1969; Metzger, 1970; Gaily, 1973; Cathou and Dorrington, 1975). The molecule consists of pairs of identical chains, two light (L) and two heavy (H). The basic early work of Porter (1959) showed that mild proteolysis would cleave the molecule into three fragments of roughly equal molecular weight, two Fabs and one Fc. This cleavage is now known to occur in the middle of the H chain in a “hinge” region that is particularly susceptible to proteolytic attack. The hinge region contains about 25 amino acids and frequently contains large amounts of proline. It permits a considerable degree of segmental flexibility in the intact molecule, allowing the Fab portions of some immunoglobulins to pivot with respect to the Fc in such a way that the molecule can assume a variety of shapes from an acute Y to a T (see Metzger, 1974).
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Davies, D.R., Padlan, E.A., Segal, D.M. (1975). Immunoglobulin Structures at High Resolution. In: Inman, F.P., Mandy, W.J. (eds) Contemporary Topics in Molecular Immunology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8930-3_5
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