DRB1*1316: evolutionary and functional implications of a novel polymorphism at codon 86.
HLA-DRB1 molecules contain extensive polymorphism localized to specific functional regions of the antigen binding site (ABS). Position 86 of HLA-DRB1 molecules modulates a hydrophobic pocket in the ABS which acts as a peptide anchoring site [1]. We report the nucleotide sequence of HLA-DRB1*1316 which is identical to HLA-DRB1*1301 and *1302 except at codon 86. The novel allele encodes aspartate rather than valine or glycine at position 86. Val86 and Gly86 have been exclusively observed in thousands of oligotyped specimens; thus Asp86 is a rare polymorphism which is significant with respect to hypotheses concerning evolution and structure-function relationships of HLA-DRB1 molecules.
Dinauer
D M
DM
Blood Center of Southeastern Wisconsin, Milwaukee, USA.
Glumm
R
R
Baxter-Lowe
L A
LA
D000483:Alleles; D000818:Animals; D001224:Aspartic Acid / Q000235:genetics; D001483:Base Sequence; D003062:Codon / Q000276:immunology*; D019143:Evolution, Molecular; D005998:Glycine / Q000235:genetics; D006684:HLA-DR Antigens / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology*; D059811:HLA-DRB1 Chains; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011110:Polymorphism, Genetic / Q000276:immunology*; D011323:Primates; D014633:Valine / Q000235:genetics
D003062:Codon; D006684:HLA-DR Antigens; D059811:HLA-DRB1 Chains; D001224:Aspartic Acid; D014633:Valine; D005998:Glycine