2rri

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[[Image:2rri.png|left|200px]]
 
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==NMR structure of vasoactive intestinal peptide in DPC Micelle==
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The line below this paragraph, containing "STRUCTURE_2rri", creates the "Structure Box" on the page.
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<StructureSection load='2rri' size='340' side='right'caption='[[2rri]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2rri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rri OCA], [https://pdbe.org/2rri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rri RCSB], [https://www.ebi.ac.uk/pdbsum/2rri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rri ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_2rri| PDB=2rri | SCENE= }}
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== Function ==
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[https://www.uniprot.org/uniprot/VIP_HUMAN VIP_HUMAN] VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.<ref>PMID:15013843</ref> PHM and PHV also cause vasodilation. PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin.<ref>PMID:15013843</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Vasoactive intestinal peptide (VIP) is a 28-amino acid neuropeptide which belongs to a glucagon/secretin superfamily, the ligand of class II G protein-coupled receptors. Knowledge for the conformation of VIP bound to membrane is important because the receptor activation is initiated by membrane binding of VIP. We have previously observed that VIP-G (glycine-extended VIP) is unstructured in solution, as evidenced by the limited NMR chemical shift dispersion. In this study, we determined the three-dimensional structures of VIP-G in two distinct membrane-mimicking environments. Although these are basically similar structures composed of a disordered N-terminal region and a long alpha-helix, micelle-bound VIP-G has a curved alpha-helix. The side chains of residues Phe(6), Tyr(10), Leu(13), and Met(17) found at the concave face form a hydrophobic patch in the micelle-bound state. The structural differences in two distinct membrane-mimicking environments show that the micelle-bound VIP-G localized at the water-micelle boundary with these side chains toward micelle interior. In micelle-bound PACAP-38 (one of the glucagon/secretin superfamily peptide) structure, the identical hydrophobic residues form the micelle-binding interface. This result suggests that these residues play an important role for the membrane binding of VIP and PACAP.
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===NMR structure of vasoactive intestinal peptide in DPC Micelle===
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Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments.,Umetsu Y, Tenno T, Goda N, Shirakawa M, Ikegami T, Hiroaki H Biochim Biophys Acta. 2011 May;1814(5):724-30. Epub 2011 Mar 23. PMID:21439408<ref>PMID:21439408</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_21439408}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2rri" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 21439408 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21439408}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2rri]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRI OCA].
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==Reference==
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<ref group="xtra">PMID:021439408</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Goda, N.]]
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[[Category: Large Structures]]
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[[Category: Hiroaki, H.]]
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[[Category: Goda N]]
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[[Category: Ikegami, T.]]
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[[Category: Hiroaki H]]
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[[Category: Shirakawa, M.]]
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[[Category: Ikegami T]]
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[[Category: Tenno, T.]]
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[[Category: Shirakawa M]]
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[[Category: Umetsu, Y.]]
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[[Category: Tenno T]]
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[[Category: Hormone]]
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[[Category: Umetsu Y]]

Current revision

NMR structure of vasoactive intestinal peptide in DPC Micelle

PDB ID 2rri

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