Complete amino acid sequence of pooled papain-solubilized HLA-A, -B, and -C antigens: relatedness to immunoglobulins and internal homologies.
Pooled, papain-solubilized HLA-A, -B, and -C antigens, derived from a large number of individuals and comprising several allelic forms, have been subjected to amino acid sequence determination. Despite the heterogeneity of the material, a main sequence representing all of the 273 amino acid residues could be established. The primary structure encompasses two immunoglobulin-like disulfide loops. The single carbohydrate moiety is attached to asparagine-86. Computer analyses demonstrated that the COOH-terminal one-third of the sequence, called H3, display statistically significant homology with members of the immunoglobulin family. The NH2-terminal two-thirds of the molecule, called H1 and H2, are not significantly homologous to any of the immunoglobulin sequences. However, H1 and H2 exhibit a distant relatedness to each other but no obvious similarity to the H3 region.
D000595:Amino Acid Sequence; D000818:Animals; D003201:Computers; D006183:H-2 Antigens; D006680:HLA Antigens; D006801:Humans; D007136:Immunoglobulins; D046911:Macromolecular Substances; D051379:Mice; D010206:Papain / Q000378:metabolism; D010446:Peptide Fragments; D012995:Solubility
D006183:H-2 Antigens; D006680:HLA Antigens; D007136:Immunoglobulins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D010206:Papain