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| ==NMR structure of vasoactive intestinal peptide in Methanol== | | ==NMR structure of vasoactive intestinal peptide in Methanol== |
| <StructureSection load='2rrh' size='340' side='right'caption='[[2rrh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='2rrh' size='340' side='right'caption='[[2rrh]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2rrh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRH FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2rrh]] 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=2RRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRH FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrh OCA], [http://pdbe.org/2rrh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rrh RCSB], [http://www.ebi.ac.uk/pdbsum/2rrh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrh ProSAT]</span></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=2rrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rrh OCA], [https://pdbe.org/2rrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rrh RCSB], [https://www.ebi.ac.uk/pdbsum/2rrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rrh ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://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> | | [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> |
| <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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| 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2rrh" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Goda, N]] | | [[Category: Goda N]] |
| [[Category: Hiroaki, H]] | | [[Category: Hiroaki H]] |
| [[Category: Ikegami, T]] | | [[Category: Ikegami T]] |
| [[Category: Tenno, T]] | | [[Category: Tenno T]] |
| [[Category: Umetsu, Y]] | | [[Category: Umetsu Y]] |
| [[Category: Hormone]]
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| [[Category: Peptide hormone]]
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