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

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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]

References

  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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