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• W2018889478 abstract "Class II major histocompatibility complex (MHCII) molecules present antigens to CD4(+) T cells. In addition to the most commonly studied human MHCII isotype, HLA-DR, whose beta chain is encoded by the HLA-DRB1 locus, several other isotypes that use the same alpha chain but have beta chains encoded by other genes. These other DR molecules also are expressed in antigen-presenting cells and are known to participate in peptide presentation to T cells and to be recognized as alloantigens by other T cells. Like some of the HLA-DRB1 alleles, several of these alternate DR molecules have been associated with specific autoimmune diseases and T cell hypersensitivity. Here we present the structure of an HLA-DR molecule (DR52c) containing one of these alternate beta chains (HLA-DRB3*0301) bound to a self-peptide derived from the Tu elongation factor. The molecule shares structurally conserved elements with other MHC class II molecules but has some unique features in the peptide-binding groove. Comparison of the three major HLA-DBR3 alleles (DR52a, b, and c) suggests that they were derived from one another by recombination events that scrambled the four major peptide-binding pockets at peptide positions 1, 4, 6, and 9 but left virtually no polymorphisms elsewhere in the molecules." @default.
• W2018889478 created "2016-06-24" @default.
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• W2018889478 date "2008-08-19" @default.
• W2018889478 modified "2023-10-18" @default.
• W2018889478 title "The structure of HLA-DR52c: Comparison to other HLA-DRB3 alleles" @default.
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• W2018889478 doi "https://doi.org/10.1073/pnas.0805810105" @default.
• W2018889478 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2515224" @default.
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