1OF2
Crystal structure of HLA-B*2709 complexed with the vasoactive intestinal peptide type 1 receptor (VIPR) peptide (residues 400-408)
Summary for 1OF2
| Entry DOI | 10.2210/pdb1of2/pdb |
| Related | 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1AKJ 1AO7 1CE6 1DE4 1E27 1E28 1EFX 1EXU 1GZP 1GZQ 1HHG 1HHH 1HHI 1HHJ 1HHK 1HLA 1HSA 1HSB 1I4F 1I7R 1I7T 1I7U 1IM3 1IM9 1JF1 1JGE 1JHT 1JNJ 1K5N 1KPR 1KTL 1LDS 1OGA 1OGT 1QLF 1QQD 1TMC 2CLR 2HLA 3HLA |
| Descriptor | HUMAN LYMPHOCYTE ANTIGEN HLA-B27, BETA-2-MICROGLOBULIN, VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR, ... (6 entities in total) |
| Functional Keywords | immune system, mhc (major histocompatibility complex), hla (human leukocyte antigen) |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 3 |
| Total formula weight | 45561.49 |
| Authors | Hulsmeyer, M.,Fiorillo, M.T.,Bettosini, F.,Sorrentino, R.,Saenger, W.,Ziegler, A.,Uchanska-Ziegler, B. (deposition date: 2003-04-04, release date: 2004-01-29, Last modification date: 2024-11-13) |
| Primary citation | Hulsmeyer, M.,Fiorillo, M.T.,Bettosini, F.,Sorrentino, R.,Saenger, W.,Ziegler, A.,Uchanska-Ziegler, B. Dual, Hla-B27 Subtype-Dependent Conformation of a Self-Peptide J.Exp.Med., 199:271-, 2004 Cited by PubMed Abstract: The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens. PubMed: 14734527DOI: 10.1084/JEM.20031690 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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