PDB ID or protein name

2mag » Magainin 2

2mag » Magainin 2
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Topology in Secreted
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2mag » Magainin 2
Hydrophobic Thickness or Depth 10.1 ± 0.9 Å
Tilt Angle 81 ± 14°
ΔGtransfer -13.7 kcal/mol
Links to 2mag PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution NMR
Other PDB entries representing this structure 1dum, 1f0d, 1f0f, 1f0g, 1f0h
Number of subunits 1
Experimental Verification for 2mag » Magainin 2
The alpha-helix of magainin is parallel to the membrane surface, with its nonpolar side (F5, L6, F16, I20) buried in the hydrophobic region of the membrane (Matsuzaki et al. 1994, Marassi et al. 2000). The transfer energy is strongly overestimated (~ -8 kcal/mol in the experiment, Wieprecht et al. 1999), because part of the transfer energy must be spent to fold an alpha-helix from a coil in aqueous solution, prior to insertion of the helix into membrane.
3 references
Marassi FM, Ma C, Gesell JJ, and Opella SJ. 2000. Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers. J Magn Reson PubMed
Matsuzaki K, Murase O, Tokuda H, Funakoshi S, Fujii N, and Miyajima K. 1994 Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry. 33: 3342-3349. PubMed
Wieprecht, T., Beyermann, M., and Seelig, J. 1999. Binding of antibacterial magainin peptides to electrically neutral membranes: thermodynamics and structure. Biochemistry. 38:10377-10387. PubMed
Comments on 2mag » Magainin 2
Antimicrobial peptide that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. This peptide forms oligomeric ion channels in membranes. It also forms a dimer (1dum). Side-chain conformers of this NMR model were optimized.