We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2rri

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

NMR structure of vasoactive intestinal peptide in DPC Micelle

Structural highlights

2rri is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] PHM and PHV also cause vasodilation. PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin.^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ma JN, Currier EA, Essex A, Feddock M, Spalding TA, Nash NR, Brann MR, Burstein ES. Discovery of novel peptide/receptor interactions: identification of PHM-27 as a potent agonist of the human calcitonin receptor. Biochem Pharmacol. 2004 Apr 1;67(7):1279-84. PMID:15013843 doi:http://dx.doi.org/10.1016/j.bcp.2003.11.008
↑ Ma JN, Currier EA, Essex A, Feddock M, Spalding TA, Nash NR, Brann MR, Burstein ES. Discovery of novel peptide/receptor interactions: identification of PHM-27 as a potent agonist of the human calcitonin receptor. Biochem Pharmacol. 2004 Apr 1;67(7):1279-84. PMID:15013843 doi:http://dx.doi.org/10.1016/j.bcp.2003.11.008
↑ Umetsu Y, Tenno T, Goda N, Shirakawa M, Ikegami T, Hiroaki H. Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments. Biochim Biophys Acta. 2011 May;1814(5):724-30. Epub 2011 Mar 23. PMID:21439408 doi:10.1016/j.bbapap.2011.03.009

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rri"

@@ Line 1: / Line 1: @@
 ==NMR structure of vasoactive intestinal peptide in DPC Micelle==
-<StructureSection load='2rri' size='340' side='right' caption='[[2rri]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<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 [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]. <br>
+<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><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+</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>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rri OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rri RCSB], [http://www.ebi.ac.uk/pdbsum/2rri PDBsum]</span></td></tr>
+</table>
-<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 ==
@@ Line 12: / Line 14: @@
 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 MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2rri" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 19: / Line 22: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Goda, N.]]
+[[Category: Large Structures]]
-[[Category: Hiroaki, H.]]
+[[Category: Goda N]]
-[[Category: Ikegami, T.]]
+[[Category: Hiroaki H]]
-[[Category: Shirakawa, M.]]
+[[Category: Ikegami T]]
-[[Category: Tenno, T.]]
+[[Category: Shirakawa M]]
-[[Category: Umetsu, Y.]]
+[[Category: Tenno T]]
-[[Category: Hormone]]
+[[Category: Umetsu Y]]

2rri

From Proteopedia

Current revision

NMR structure of vasoactive intestinal peptide in DPC Micelle

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox