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1ogt

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1ogt, resolution 1.47Å ()
Sites: , , , , and
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, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1ogt is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • 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
  • Hulsmeyer M, Hillig RC, Volz A, Ruhl M, Schroder W, Saenger W, Ziegler A, Uchanska-Ziegler B. HLA-B27 subtypes differentially associated with disease exhibit subtle structural alterations. J Biol Chem. 2002 Dec 6;277(49):47844-53. Epub 2002 Sep 18. PMID:12244049 doi:10.1074/jbc.M206392200
  • Madden DR, Gorga JC, Strominger JL, Wiley DC. The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC. Cell. 1992 Sep 18;70(6):1035-48. PMID:1525820

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