|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS== | | ==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=''> | + | <StructureSection load='1d7n' size='340' side='right'caption='[[1d7n]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[1d7n]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1d7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7n OCA], [https://pdbe.org/1d7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d7n RCSB], [https://www.ebi.ac.uk/pdbsum/1d7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d7n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAST_VESLE 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. | + | [https://www.uniprot.org/uniprot/MAST_VESLE 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 25: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Vespula lewisii]] | | [[Category: Vespula lewisii]] |
| - | [[Category: Aoyagi, H]] | + | [[Category: Aoyagi H]] |
| - | [[Category: Asakura, T]] | + | [[Category: Asakura T]] |
| - | [[Category: Demura, M]] | + | [[Category: Demura M]] |
| - | [[Category: Hori, Y]] | + | [[Category: Hori Y]] |
| - | [[Category: Iwadate, M]] | + | [[Category: Iwadate M]] |
| - | [[Category: Niidome, T]] | + | [[Category: Niidome T]] |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Sodium dodecyl sulfate bound conformation]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
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
|
