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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins.

The papain-solubilized fragment of the heavy chain of HLA-B7, which is the NH2-terminal part of the whole polypeptide chain, can be divided into three regions by mild acid and cyanogen bromide cleavages. The first 100 amino acids terminating in a methionine residue contain the carbohydrate moiety; this segment is followed by two others of molecular weights 9,999 and 13,000, each containing an intrachain disulfide bridge. The two intrachain disulfide bridges are separated by a stretch of amino acids containing an acid-labile aspartyl-prolHLA-2, A28, and AW25 contain this acid-labile peptide bond in their larger subunit. Sequencing from the acid cleavage site of HLA-7 through the third half-cystine revealed consideralbe homology with amino acid sequences around a half-cystine in immunoglobulin variable regions.[1]


  1. Further structural studies of the heavy chain of HLA antigens and its similarity to immunoglobulins. Terhorst, C., Robb, R., Jones, C., Strominger, J.L. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
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