期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：11
页码：5839-5842
DOI：10.1073/pnas.76.11.5839
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The classical human transplantation antigens, derived from the HLA-A, -B, and -C loci, are cell-surface-expressed glycoproteins. On the exterior of the cell the transplantation antigen heavy chain exposes two disulfide-containing domains and a glycosylated NH2-terminal extension. The disulfide-containing domain closest to the membrane has been isolated and its amino acid sequence has been determined. The HLA antigens used for the sequence analysis were derived from two and possibly three loci and comprised several allelic forms. The primary structure was remarkably invariant, and amino acid variations were observed only at three positions. Whether this suggests that the allelic variation of the HLA antigens is preferentially confined to other regions of the molecule or is a result of fortuitous selection of peptides remains to be established. The sequenced portion of the HLA antigen heavy chain is as homologous to beta 2-microglobulin and immunoglobulin light and heavy chains as are the latter to one another. This observation strengthens the notion that the transplantation antigens and the immunoglobulins are evolutionarily related.
