2mag
From Proteopedia
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|PDB= 2mag |SIZE=350|CAPTION= <scene name='initialview01'>2mag</scene> | |PDB= 2mag |SIZE=350|CAPTION= <scene name='initialview01'>2mag</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Opella, S J.]] | [[Category: Opella, S J.]] | ||
[[Category: Zasloff, M.]] | [[Category: Zasloff, M.]] | ||
| - | [[Category: NH2]] | ||
[[Category: amphipathic helix]] | [[Category: amphipathic helix]] | ||
[[Category: antibiotic]] | [[Category: antibiotic]] | ||
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[[Category: micelle]] | [[Category: micelle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:03:42 2008'' |
Revision as of 01:03, 31 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES
Overview
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.
About this Structure
2MAG is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.
Reference
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
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