X-ray diffraction analysis of crystals from the human major histocompatibility antigen HLA-B*2706 in complex with a viral peptide and with a self-peptide.
The human leukocyte antigen (HLA) alleles HLA-B*2704 and HLA-B*2706 show an ethnically restricted distribution and are differentially associated with ankylosing spondylitis, with HLA-B*2706 lacking association with this autoimmune disease. However, the products of the two alleles differ by only two amino acids, at heavy-chain residues 114 (His in HLA-B*2704; Asp in HLA-B*2706) and 116 (Asp in HLA-B*2704; Tyr in HLA-B*2706). Both residues could be involved in contacting amino acids of a bound peptide, suggesting that peptides presented by these subtypes play a role in disease pathogenesis. Two HLA-B*2706-peptide complexes were crystallized using the hanging-drop vapour-diffusion method with PEG as precipitant. Data sets were collected to resolutions of 2.70 A (viral peptide pLMP2, RRRWRRLTV; space group P2(1)2(1)2(1)) and 1.83 A (self-peptide pVIPR, RRKWRRWHL; space group P2(1)). Using HLA-B*2705 complexed with the pGR peptide (RRRWHRWRL) as a search model, unambiguous molecular-replacement solutions were found for both HLA-B*2706 complexes.
Zawacka
Anna
A
Institut für Immungenetik, Charité-Universitätsmedizin Berlin, Campus Virchow-Klinikum, Humboldt-Universität zu Berlin, Spandauer Damm 130, 14050 Berlin, Germany.
Loll
Bernhard
B
Biesiadka
Jacek
J
Saenger
Wolfram
W
Uchanska-Ziegler
Barbara
B
Ziegler
Andreas
A
D003460:Crystallization; D015235:HLA-B Antigens / Q000737:chemistry*; D015796:HLA-B27 Antigen; D006801:Humans; D010455:Peptides / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D013167:Spondylitis, Ankylosing / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D015235:HLA-B Antigens; C510629:HLA-B*27:06 antigen; D015796:HLA-B27 Antigen; D010455:Peptides; D014764:Viral Proteins; D011092:Polyethylene Glycols