1ogt | pdb_00001ogt

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Template:STRUCTURE 1ogt

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

Template:ABSTRACT PUBMED 14734527

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]

About this Structure

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

See Also

Reference

  1. 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
  2. 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
  3. 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
  1. ↑ 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

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