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Evolution of variable and constant domains and joining segments of rearranging immunoglobulins
Author(s) -
Marchalonis John J.,
Schluter Samuel F.
Publication year - 1989
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.3.13.2509274
Subject(s) - immunoglobulin light chain , biology , evolutionary biology , phylogenetic tree , immunoglobulin domain , constant (computer programming) , antibody , phylogenetics , immunoglobulin heavy chain , vertebrate , genetics , gene , computer science , programming language
The rearranging immunoglobulins (Igs) are a family of recognition and defense proteins found in all vertebrate classes. These proteins consist of two types of polypeptide chains; each of these contains a variable (V) domain, a joining (J) segment, and a constant (C) region, which can itself consist of one to four domains. The distinction betweeen light and heavy chains is an ancient one phylogenetically that is reflected in the structures of V, J, and C regions. Despite the early emergence of these genetic elements, conservatism is apparent in the peptide structures encoded by V, J, and C exons. C regions of heavy chains did not evolve as single units; rather the individual domains show their own clustering patterns, which apparently are independent of heavy‐chain designation or species. C‐region domains of light chains and the T cell receptor β chain are similar to one another and to the most carboxyl‐terminal domain of heavy chains. Comparison of the light chains of sharks, bullfrogs, chickens, and mammals indicated that a phylogenetic distinction can be made between x and λ light chains. V and J segments of the rearranging T cell receptors α, γ, and δ are homologous to the corresponding segments of Igs, but their C regions form a group that is markedly distinct from those of conventional Igs and Tcr β.—M archalonis , J. J.; S chluter , S. F. Evolution of variable and constant domains and joining segments of rearranging immunoglobulins. FASEB J. 3: 2469‐2479; 1989.