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. 1980 Feb;77(2):1129–1133. doi: 10.1073/pnas.77.2.1129

Complete amino acid sequence of pooled papain-solubilized HLA-A, -B, and -C antigens: relatedness to immunoglobulins and internal homologies.

L Trägärdh, L Rask, K Wiman, J Fohlman, P A Peterson
PMCID: PMC348438  PMID: 6928663

Abstract

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.

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Selected References

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