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The generation of antibody diversity
Author(s) -
Rose David R.
Publication year - 1982
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830130111
Subject(s) - gene , immunoglobulin light chain , recombination , genetics , biology , gene conversion , antibody , point mutation , sequence (biology) , somatic cell , peptide sequence , immunoglobulin heavy chain , microbiology and biotechnology , mutation
By their nature, antibody molecules exhibit a wide range of binding specificities. The antigen‐binding properties of the antibody reside entirely in the amino‐terminal portion of the molecule, termed the variable domain. Structurally, the combining site specificity is determined by the amino‐acid residues within 6 short lengths, 3 each in the heavy and light chains, of unusually variable sequence. The hypervariability of 2 of these lengths arises from the somatic recombination of short gene segments into a single stretch of mRNA which encodes the entire variable region of 1 polypeptide chain. For example, a V gene segment that codes for most of the variable portion of a light chain, can combine with one of a number of much shorter J gene segments to create the complete variable region gene. In heavy chain genes, a third element, the D gene segment, increases the potential for diversity even further. A mechanism has been proposed by which variability occurs at the point where 2 gene segments join. Thus, a large part of the generation of antibody diversity occurs in the somatic recombination of small genetic elements.