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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.
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
January 1979,
Scandinavian journal of immunology,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
December 1979,
Biochemistry,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
June 1979,
Transplantation proceedings,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
January 1978,
Scandinavian journal of immunology,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
October 1982,
Biochemistry,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
June 1982,
Proceedings of the National Academy of Sciences of the United States of America,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
January 1980,
Scandinavian journal of immunology,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
December 1979,
Biochemistry,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
March 2007,
Internal and emergency medicine,
L Trägärdh, and
L Rask, and
K Wiman, and
J Fohlman, and
P A Peterson
May 1979,
Blood,
