2MAG

NMR STRUCTURE OF MAGAININ 2 IN DPC MICELLES, 10 STRUCTURES

2MAG の概要

• エントリーDOI: 10.2210/pdb2mag/pdb
• 分子名称: MAGAININ 2 (1 entity in total)
• 機能のキーワード: antibiotic, magainin, membrane, amphipathic helix, micelle
• 由来する生物種: Xenopus laevis (African clawed frog)
• 細胞内の位置: Secreted: P11006
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2469.95

構造登録者

Gesell, J.J.,Zasloff, M.,Opella, S.J. (登録日: 1997-12-19, 公開日: 1998-04-08, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

SOLUTION NMR