| Structural highlights
1ogt is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| 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, 1mi5, 1of2, 1oga, 1qlf, 1qqd, 1tmc, 2clr, 2hla, 3hla |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[1B18_HUMAN] Involved in the presentation of foreign antigens to the immune system. [VIPR1_HUMAN] This is a receptor for VIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The affinity is VIP = PACAP-27 > PACAP-38.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Dual, HLA-B27 subtype-dependent conformation of a self-peptide.,Hulsmeyer M, Fiorillo MT, Bettosini F, Sorrentino R, Saenger W, Ziegler A, Uchanska-Ziegler B J Exp Med. 2004 Jan 19;199(2):271-81. PMID:14734527[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xia M, Sreedharan SP, Goetzl EJ. Predominant expression of type II vasoactive intestinal peptide receptors by human T lymphoblastoma cells: transduction of both Ca2+ and cyclic AMP signals. J Clin Immunol. 1996 Jan;16(1):21-30. PMID:8926282
- ↑ Hulsmeyer M, Fiorillo MT, Bettosini F, Sorrentino R, Saenger W, Ziegler A, Uchanska-Ziegler B. Dual, HLA-B27 subtype-dependent conformation of a self-peptide. J Exp Med. 2004 Jan 19;199(2):271-81. PMID:14734527 doi:10.1084/jem.20031690
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