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Evolution of Vertebrate Immunoglobulin Variable Gene Segments

2000; Springer Science+Business Media; Linguagem: Inglês

10.1007/978-3-642-59674-2_10

2196-9965

Tatsuya Ota, T. Ya. Sitnikova, M Nei,

Glycosylation and Glycoproteins Research

Immunoglobulins (Igs), also known as antibodies, play major roles in the verte- brate humoral immune system. They recognize and bind to foreign antigens, such as viruses, bacteria and parasites, and initiate a series of immunological responses (effector function). The dual function of the Ig protein is facilitated by its unique structure consisting of two functionally distinct domains, i.e., the variable (V) domain for antigen recognition and the constant (C) domain for effector function (Frazer and Capra 1998). Ig is generally composed of two identical heavy (IgH) and two identical light (IgL) chains, both of which contribute to the formation of V and C domains.