Abstract
The major histocompatibility complex in vertebrates consists of a number of closely linked genetic loci that encode a variety of cell-surface glycoproteins and serum proteins known as histocompatibility antigens (Klein, 1975). Through these antigens, the cells of the immune system interact and thus regulate the antibody and cellular immune response to foreign antigens (Zinkernagel and Doherty, 1974; Klein, 1979). Biochemically, these antigens have been subdivided into three classes on the basis of structural and functional homology (Ploegh et al., 1981). Thus, the class I antigens (HLA-A, B, C; H2K, D, L) are cell-surface glycoproteins composed of two polypeptide subunits. The heavy chain carries the antigenic determinants and is in noncovalent association with β2-microglobulin. Similarly, the class II antigens are also composed of two polypeptide chains. Significant features of these antigens are that they are highly polymorphic within the population. At least 35 alleles are known at the HLA-B locus, 20 at the HLA-A locus, and fewer than 10 at the HLA-C locus. In the mouse, the extent of polymorphism at the class I loci is even higher; i.e., close to 100 alleles at both the H2-K and -D loci. In contrast, the polymorphism at the HLA-D locus is only beginning to be uncovered with recent definitions of multiple loci encoding these antigens (Tanigachi et al.,1980; Shaw et al., 1981; Shackelford et al., 1981).
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© 1984 Plenum Press, New York
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Sood, A.K. et al. (1984). Cloning and Structure Analysis of Histocompatibility Class I and Class II Genes. In: Kumar, A. (eds) Eukaryotic Gene Expression. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7459-6_5
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DOI: https://doi.org/10.1007/978-1-4684-7459-6_5
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