Abstract
The ancestral gene for immunoglobulin light-chain variable regions (Ig VLs) of the kappa as well as the lambda class apparently arose from about 12 tandem repeats of the 48-base-long primordial building block sequence TCT-TGC-GCA-GTA-AGT-CCA-CTC-CAG-GTC-ATA-TCC-AGT-CAG-GCT-GCT-GAA. Even today, amino acid residues 67 to 82 of each Ig V kappa L are still specified by a direct descendant in toto of the above-noted primordial building block, whereas amino acid residues 14 to 25 are invariably specified by its truncated copy. The Ig VL primordial building block presently identified is 100% complementary to the Ig VH (heavy-chain variable region) primordial building block previously identified. In the recognition of specific antigenic determinants by antibodies, Ig VL and Ig VH of light-chain--heavy-chain dimers have to complement each other. It is perhaps fitting that the primordial building blocks of the two are represented by the complementary strands of the same 48-base-pair-long DNA sequence.
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Selected References
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