Nature of polymorphism in HLA-A, -B, and -C molecules
- PMID: 3375250
- PMCID: PMC280349
- DOI: 10.1073/pnas.85.11.4005
Nature of polymorphism in HLA-A, -B, and -C molecules
Abstract
Diversity in 39 HLA-A, -B, and -C molecules is derived from 20 amino acid positions of high variability and 71 positions of low variability. Variation in the structurally homologous alpha 1 and alpha 2 domains is distinct and may correlate with partial segregation of peptide and T-cell receptor binding functions. Comparison of 15 HLA-A with 20 HLA-B molecules reveals considerable locus-specific character, due primarily to differences at polymorphic residues. The results indicate that genetic exchange between alleles of the same locus has been a more important mechanism in the generation of HLA-A, -B, and -C diversity than genetic exchange events between alleles of different loci.
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