Title : The
structure of HLA-DR52c: comparison to other
HLA-DRB3 alleles
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 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
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*Output_Site_Fusion* (sent_index,
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