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Major histocompatibility complex, class II, DP beta 1
HLA-DPB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DPA) and a beta chain (DPB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DP molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules. [provided by RefSeq, Jul 2008] (from
International Histocompatibility Working Group in Hematopoietic Cell Transplantation et al., Milano, Italy. In Lancet Oncol, 2012
Avoidance of an unrelated donor with a non-permissive T-cell-epitope mismatch at HLA-DPB1 might provide a practical clinical strategy for lowering the risks of mortality after unrelated-donor haemopoietic-cell transplantation.
de Bakker et al., Boston, United States. In Nat Genet, 2012
Three amino acid positions (11, 71 and 74) in HLA-DRbeta1 and single-amino-acid polymorphisms in HLA-B (position 9) and HLA-DPbeta1 (position 9), all located in peptide-binding grooves, almost completely explain MHC association to rheumatoid arthritis risk.