3C5J

Crystal structure of HLA DR52c

Summary for 3C5J

• Entry DOI: 10.2210/pdb3c5j/pdb
• Descriptor: HLA class II histocompatibility antigen, DR alpha chain, MHC class II antigen, Elongation factor 1-alpha 2, ... (6 entities in total)
• Functional Keywords: hla, mhc class ii, glycoprotein, immune response, membrane, mhc ii, transmembrane, elongation factor, gtp-binding, methylation, nucleotide-binding, nucleus, phosphoprotein, protein biosynthesis, membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 45135.61

Authors

Dai, S.,Kappler, J.W. (deposition date: 2008-01-31, release date: 2008-08-05, Last modification date: 2024-10-30)

Primary citation

Dai, S.,Crawford, F.,Marrack, P.,Kappler, J.W.
The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles.
Proc.Natl.Acad.Sci.USA, 105:11893-11897, 2008

PubMed 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.

PubMed: 18697946
DOI: 10.1073/pnas.0805810105

Experimental method

X-RAY DIFFRACTION (1.8 Å)