Evolutionary relationship between HLA-DR antigen beta-chains, HLA-A, B, C antigen subunits and immunoglobulin chains.
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Larhammar D, Wiman K, Schenning L, Claesson L, Gustafsson K, Peterson PA, Rask L
Evolutionary relationship between HLA-DR antigen beta-chains, HLA-A, B, C antigen subunits and immunoglobulin chains.
Scand J Immunol. 1981 Dec;14(6):617-22.
- PubMed ID
- 6952552 [ View in PubMed]
- Abstract
cDNA for a beta-chain of HLA-DR antigens was cloned and the partial nucleotide sequence was determined. The data suggest that the beta-chain consists of approximately 230 amino acids, of which about 200 are exposed on the cell surface. The beta-chain appears to be composed of two exposed disulphide-containing domains. The arrangement of the disulphide loops suggests that the beta-chain is similar in structure to the HLA-A, B, C antigen subunits and the immunoglobulin chains. For the beta-chain domain closest to the membrane this similarity was verified at the level of primary structure. The partial amino acid sequence of the NH2-terminal domain did not display any apparent homology to HLA-A, B, C antigens and immunoglobulins. However, the similarity established here between the two types of major histocompatibility antigen subunits and the immunoglobulin chains suggests a common ancestral origin for at least some regions of these molecules.