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2mag

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[[Image:2mag.gif|left|200px]]
 
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{{Structure
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==NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES==
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|PDB= 2mag |SIZE=350|CAPTION= <scene name='initialview01'>2mag</scene>
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<StructureSection load='2mag' size='340' side='right'caption='[[2mag]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
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<table><tr><td colspan='2'>[[2mag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAG FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<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>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mag OCA], [https://pdbe.org/2mag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mag RCSB], [https://www.ebi.ac.uk/pdbsum/2mag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mag ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mag OCA], [http://www.ebi.ac.uk/pdbsum/2mag PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2mag RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/MAGA_XENLA MAGA_XENLA] Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain cell membranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure of the peptide in three of the membrane environments most commonly employed in biophysical studies. Sequence-specific resonance assignments were determined for the peptide in perdeuterated dodecylphosphocholine (DPC) and sodium dodecylsulfate micelles and confirmed for the peptide in 2,2,2-trifluoroethanol solution. The secondary structure is shown to be helical in all of the solvent systems. The NMR data were used as a set of restraints for a simulated annealing protocol that generated a family of three-dimensional structures of the peptide in DPC micelles, which superimposed best between residues 4 and 20. For these residues, the mean pairwise rms difference for the backbone atoms is 0.47 +/- 0.10 A from the average structure. The calculated peptide structures appear to be curved, with the bend centered at residues Phe12 and Gly13.
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'''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES'''
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Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.,Gesell J, Zasloff M, Opella SJ J Biomol NMR. 1997 Feb;9(2):127-35. PMID:9090128<ref>PMID:9090128</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mag" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic gradient across certain cell membranes. Two-dimensional 1H NMR spectroscopy was used to investigate the structure of the peptide in three of the membrane environments most commonly employed in biophysical studies. Sequence-specific resonance assignments were determined for the peptide in perdeuterated dodecylphosphocholine (DPC) and sodium dodecylsulfate micelles and confirmed for the peptide in 2,2,2-trifluoroethanol solution. The secondary structure is shown to be helical in all of the solvent systems. The NMR data were used as a set of restraints for a simulated annealing protocol that generated a family of three-dimensional structures of the peptide in DPC micelles, which superimposed best between residues 4 and 20. For these residues, the mean pairwise rms difference for the backbone atoms is 0.47 +/- 0.10 A from the average structure. The calculated peptide structures appear to be curved, with the bend centered at residues Phe12 and Gly13.
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*[[Magainin 2|Magainin 2]]
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== References ==
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==About this Structure==
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<references/>
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2MAG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAG OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution., Gesell J, Zasloff M, Opella SJ, J Biomol NMR. 1997 Feb;9(2):127-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9090128 9090128]
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[[Category: Single protein]]
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[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Gesell, J J.]]
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[[Category: Gesell JJ]]
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[[Category: Opella, S J.]]
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[[Category: Opella SJ]]
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[[Category: Zasloff, M.]]
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[[Category: Zasloff M]]
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[[Category: amphipathic helix]]
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[[Category: antibiotic]]
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[[Category: magainin]]
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[[Category: membrane]]
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[[Category: micelle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:03:42 2008''
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Current revision

NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES

PDB ID 2mag

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