Open AccessComplete amino acid sequence of an HLA-DR antigen-like beta chain as predicted from the nucleotide sequence: similarities with immunoglobulins and HLA-A, -B, and -C antigens.
Author(s) -
Dan Larhammar,
L. Schenning,
Kenth Gustafsson,
Klas G. Wiman,
Lena Claesson,
Lars Rask,
Per A. Peterson
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.12.3687
Subject(s) - asparagine , peptide sequence , immunoglobulin heavy chain , microbiology and biotechnology , biology , antigen , immunoglobulin light chain , nucleic acid sequence , human leukocyte antigen , complementary dna , antibody , biochemistry , amino acid , chemistry , genetics , gene
The complete nucleotide sequence of an HLA-DR antigen-like beta-chain cDNA clone was determined. The 1,080 base pairs include the complete coding region and most of the untranslated portion. The predicted amino acid sequence has 229 residues. The beta chain contains two immunoglobulin-like disulfide loops and a 21-amino acid residue membrane-integrated segment. Ten amino acid residues reside on the cytoplasmic side of the plasma membrane. The single asparagine-linked carbohydrate moiety is attached to asparagine-19. The NH2-terminal 91 residues of the beta chain are homologous to the corresponding region of HLA-A, -B, and -C antigen heavy chains. Residues 92-192 of the beta chain display statistically significant homology to members of the immunoglobulin family, beta 2-microglobulin, and the immunoglobulin-like domain of HLA-A, -B, and -C antigen heavy chains. These data establish that the major histocompatibility antigens of class I and class II type and the constant regions of immunoglobulins are evolutionarily related.