HLA-DR, like other MHC class II molecules, is a transmembrane glycoprotein composed of a 36 kDa alpha chain (DRA) and 27 kDa beta chain (DRB). The alpha chain gene contains 5 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, and exon 4 encodes the transmembrane domain and the cytoplasmic tail. DRA does not have polymorphisms in the peptide binding part and acts as the sole alpha chain for DRB1, DRB3, DRB4 and DRB5. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Hundreds of DRB1 alleles have been described and typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. HLA-DR is expressed primarily on antigen presenting cells such as B lymphocytes, monocytes, macrophages, thymic epithelial cells and activated T lymphocytes. Three loci, DR, DQ and DP, encode the major expressed products of the human class II region. The human MHC class II molecules bind intracellularly processed peptides, present them to T-helper cells, and have a critical role in the initiation of the immune response.
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Protein Aliases: DASS-397D15.1; DR alpha chain; FLJ51114; histocompatibility antigen HLA-DR alpha; HLA class II histocompatibility antigen; HLA class II histocompatibility antigen, DR alpha chain; HLA-DRA1; MHC cell surface glycoprotein; MHC class II antigen DRA; MLRW
Gene Aliases: HLA-DRA; HLA-DRA1; MLRW
UniProt ID: (Human) P01903
Entrez Gene ID: (Human) 3122