1ogt

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[[Image:1ogt.png|left|200px]]
 
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{{STRUCTURE_1ogt| PDB=1ogt | SCENE= }}
{{STRUCTURE_1ogt| PDB=1ogt | SCENE= }}
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===CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)===
===CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)===
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{{ABSTRACT_PUBMED_14734527}}
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{{ABSTRACT_PUBMED_14734527}}
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==Function==
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[[http://www.uniprot.org/uniprot/1B18_HUMAN 1B18_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/VIPR1_HUMAN 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.<ref>PMID:8926282</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:014734527</ref><ref group="xtra">PMID:012244049</ref><ref group="xtra">PMID:001525820</ref><references group="xtra"/>
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<ref group="xtra">PMID:014734527</ref><ref group="xtra">PMID:012244049</ref><ref group="xtra">PMID:001525820</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bettosini, F.]]
[[Category: Bettosini, F.]]

Revision as of 05:17, 25 March 2013

Template:STRUCTURE 1ogt

Contents

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

  • 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
  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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