Journal
JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY
Volume 125, Issue 2, Pages S41-S52Publisher
MOSBY-ELSEVIER
DOI: 10.1016/j.jaci.2009.09.046
Keywords
Antibody structure; antibody function; immunoglobulin structure; immunoglobulin function; immunoglobulin gene rearrangement; class switching; somatic hypermutation
Categories
Funding
- National Institutes of Health/National Institute of Allergy and Infectious Diseases
- United States Immunodeficiency Network
- NABI Pharmaceuticals
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Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains. They can be separated functionally into variable domains that bind antigens and constant domains that specify effector functions, such as activation of complement or binding to Fc receptors. The variable domains are created by means of a complex series of gene rearrangement events and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation. Each variable domain can be split into 3 regions of sequence variability termed the complementarity-determining regions (CDRs) and 4 regions of relatively constant sequence termed the framework regions. The 3 CDRs of the heavy chain are paired with the 3 CDRs of the light chain to form the antigen-binding site, as classically defined. The constant domains of the heavy chain can be switched to allow altered effector function while maintaining antigen specificity. There are 5 main classes of heavy chain constant domains. Each class defines the IgM, IgG, IgA, IgD, and IgE isotypes. IgG can be split into 4 subclasses, IgG1, IgG2, IgG3, and IgG4, each with its own biologic properties, and IgA can similarly be split into IgA1 and IgA2. (J Allergy Clin Immunol 2010;125:S41-52.)
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