2rri
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==NMR structure of vasoactive intestinal peptide in DPC Micelle== | |
+ | <StructureSection load='2rri' size='340' side='right'caption='[[2rri]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <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> | ||
+ | </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> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [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;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 2rri" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Goda N]] | ||
+ | [[Category: Hiroaki H]] | ||
+ | [[Category: Ikegami T]] | ||
+ | [[Category: Shirakawa M]] | ||
+ | [[Category: Tenno T]] | ||
+ | [[Category: Umetsu Y]] |
Current revision
NMR structure of vasoactive intestinal peptide in DPC Micelle
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Categories: Homo sapiens | Large Structures | Goda N | Hiroaki H | Ikegami T | Shirakawa M | Tenno T | Umetsu Y