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New page: left|200px<br /><applet load="2mag" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mag" /> '''NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES,... |
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== | ==NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES== | ||
Magainin2 is a 23-residue antibiotic peptide that disrupts the ionic | <StructureSection load='2mag' size='340' side='right'caption='[[2mag]]' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</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='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=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> | |||
</table> | |||
== Function == | |||
[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2mag" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Magainin 2|Magainin 2]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Gesell | [[Category: Gesell JJ]] | ||
[[Category: Opella | [[Category: Opella SJ]] | ||
[[Category: Zasloff | [[Category: Zasloff M]] | ||
