Structure and function of immunoglobulins.
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TLDR
Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains that 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.Abstract:
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.read more
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References
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Journal ArticleDOI
Somatic generation of antibody diversity
TL;DR: In the genome of a germ-line cell, the genetic information for an immunoglobulin polypeptide chain is contained in multiple gene segments scattered along a chromosome which are assembled by recombination which leads to the formation of a complete gene.
Journal ArticleDOI
Naturally occurring antibodies devoid of light chains
Cécile Hamers-Casterman,Touriya Atarhouch,Serge Muyldermans,Gene E. Robinson,Hamers C,Songa Eb,Bendahman N,Raymond Hamers +7 more
TL;DR: The presence of considerable amounts of IgG-like material of Mr 100K in the serum of the camel, which is composed of heavy-chain dimers and devoid of light chains, but nevertheless have an extensive antigen-binding repertoire, opens new perspectives in the engineering of antibodies.
Journal ArticleDOI
Canonical structures for the hypervariable regions of immunoglobulins
TL;DR: The relatively few residues that, through their packing, hydrogen bonding or the ability to assume unusual phi, psi or omega conformations, are primarily responsible for the main-chain conformations of the hypervariable regions are identified.
Journal ArticleDOI
The Immunoglobulin Superfamily—Domains for Cell Surface Recognition
and A F Williams,A N Barclay +1 more
TL;DR: The domain hypothesis was firmly established when the structures of V and C domains were determined to reveal a common fold forming a sandwich of two p-sheets that was stabilized by the conserved disulfide bond.
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