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  • Title: Peptide-binding characteristics of the novel allele DRB1*0112 are probably identical to DRB1*0101.
    Author: Horn PA, DeLuca DS, Mueller K, Blasczyk R.
    Journal: Tissue Antigens; 2005 May; 65(5):505-6. PubMed ID: 15853910.
    Abstract:
    So far 11 different amino acid variants of the HLA-DRB1*01 family have been reported. We here describe the identification of a new HLA-DRB1*01 allele in a healthy female Caucasian. The allele was detected by sequencing-based typing during high-resolution typing of a potential unrelated donor from the North German Bone Marrow Registry (NKR). Compared with DRB1*010101, to which it is closest, the new variant is characterized by a new replacement mutation (G-->T) at nucleotide position 202 of exon 2, resulting in the amino acid substitution Arg-->Leu at position 72. Because this amino acid position is not involved in peptide binding or T-cell interaction, it is likely to represent a permissive mismatch to the more common HLA-DRB1*0101 allele.
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