2MAG

NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES

Summary for 2MAG

• Entry DOI: 10.2210/pdb2mag/pdb
• Descriptor: MAGAININ 2 (1 entity in total)
• Functional Keywords: antibiotic, magainin, membrane, amphipathic helix, micelle
• Biological source: Xenopus laevis (African clawed frog)
• Cellular location: Secreted: P11006
• Total number of polymer chains: 1
• Total formula weight: 2469.95

Authors

Gesell, J.J.,Zasloff, M.,Opella, S.J. (deposition date: 1997-12-19, release date: 1998-04-08, Last modification date: 2024-10-30)

Primary citation

Gesell, J.,Zasloff, M.,Opella, S.J.
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.
J.Biomol.NMR, 9:127-135, 1997

PubMed Abstract: 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.

PubMed: 9090128
DOI: 10.1023/A:1018698002314

Experimental method

SOLUTION NMR