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1d7n

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Revision as of 04:13, 30 August 2017

SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS

Structural highlights

1d7n is a 1 chain structure with sequence from Vespula lewisii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MAST_VESLE] Mast cell degranulating peptide. Activates G proteins that couple to phospholipase C. May be able to switch from an in-plane to a transmembrane orientation in lipid bilayers.

Publication Abstract from PubMed

Several complementary NMR approaches were used to study the interaction of mastoparan, a 14-residue peptide toxin from wasp venom, with lipid membranes. First, the 3D structure of mastoparan was determined using 1H-NMR spectroscopy in perdeuterated (SDS-d25) micelles. NOESY experiments and distance geometry calculations yielded a straight amphiphilic alpha-helix with high-order parameters, and the chemical shifts of the amide protons showed a characteristic periodicity of 3-4 residues. Secondly, solid-state 2H-NMR spectoscopy was used to describe the binding of mastoparan to lipid bilayers, composed of headgroup-deuterated dimyristoylglycerophosphocholine (DMPC-d4) and dimyristoylphosphatidylglycerol (DMPG). By correlating the deuterium quadrupole splittings of the alpha-segments and beta-segments, it was possible to differentiate the electrostatically induced structural response of the choline headgroup from dynamic effects induced by the peptide. A partial phase separation was observed, leading to a DMPG-rich phase and a DMPG-depleted phase, each containing some mastoparan. Finally, the insertion and orientation of a specifically 15N-labeled mastoparan (at position Ala10) in the bilayer environment was investigated by solid-state 15N-NMR spectroscopy, using macroscopically oriented samples. Two distinct orientational states were observed for the mastoparan helix, namely an in-plane and a trans-membrane alignment. The two populations of 90% in-plane and 10% trans-membrane helices are characterized by a mosaic spread of +/- 30 degrees and +/- 10 degrees, respectively. The biological activity of mastoparan is discussed in terms of a pore-forming model, as the peptide is known to be able to induce nonlamellar phases and facilitate a flip-flop between the monolayers.

Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in oriented lipid bilayers.,Hori Y, Demura M, Iwadate M, Ulrich AS, Niidome T, Aoyagi H, Asakura T Eur J Biochem. 2001 Jan;268(2):302-9. PMID:11168364^[1]

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

References

↑ Hori Y, Demura M, Iwadate M, Ulrich AS, Niidome T, Aoyagi H, Asakura T. Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in oriented lipid bilayers. Eur J Biochem. 2001 Jan;268(2):302-9. PMID:11168364

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/1d7n"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS==
 <StructureSection load='1d7n' size='340' side='right' caption='[[1d7n]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1d7n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vespula_lewisii Vespula lewisii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D7N FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7n OCA], [http://pdbe.org/1d7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d7n RCSB], [http://www.ebi.ac.uk/pdbsum/1d7n PDBsum]</span></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=1d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7n OCA], [http://pdbe.org/1d7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d7n RCSB], [http://www.ebi.ac.uk/pdbsum/1d7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d7n ProSAT]</span></td></tr>
 </table>
 == Function ==

1d7n

From Proteopedia

Revision as of 04:13, 30 August 2017

SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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