Nature of polymorphism in HLA-A, -B, and -C molecules.
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.
Parham
P
P
Department of Cell Biology, Stanford University School of Medicine, CA 94305.
Lomen
C E
CE
Lawlor
D A
DA
Ways
J P
JP
Holmes
N
N
Coppin
H L
HL
Salter
R D
RD
Wan
A M
AM
Ennis
P D
PD
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D005075:Biological Evolution; D005796:Genes; D006680:HLA Antigens / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D011995:Recombination, Genetic
D006680:HLA Antigens