HLA class I polymorphism: Structure and function and still questions

The HLA-A, HLA-B and HLA-C molecules have turned out to be highly polymorphic and functionally complex. They not only serve as peptide receptors, but also interact with beta(2)-microglobulin, an alpha beta T cell receptor, CD8 and NK inhibitory molecules, all at different sites. The fact that more than 300 class I alleles have now been defined prompted us to ask the question of where polymorphism really occurs in a class I molecule. We have used a database of 275 HLA-A, HLA-B and HLA-C alleles to illustrate how extensive the polymorphism is. The data is presented here for comparison of alleles and allele families and to facilitate studies of class I structure and function. (C) American Society for Histocompatibility and Immunogenetics, 1997. Published by Elsevier Science Inc.