1dum
From Proteopedia
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[[Image:1dum.gif|left|200px]] | [[Image:1dum.gif|left|200px]] | ||
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'''NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES''' | '''NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DUM is a [[Single protein]] structure | + | 1DUM is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Takeda, A.]] | [[Category: Takeda, A.]] | ||
[[Category: Wakamatsu, K.]] | [[Category: Wakamatsu, K.]] | ||
| - | [[Category: | + | [[Category: Amphipathic helix]] |
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Bilayer]] |
| - | [[Category: | + | [[Category: Dimer]] |
| - | [[Category: | + | [[Category: Magainin]] |
| - | [[Category: | + | [[Category: Membrane]] |
| - | [[Category: | + | [[Category: Vesicle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:17:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 11:17, 2 May 2008
NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES
Overview
To elucidate the effects of peptide dimerization on pore formation by magainin 2 (MG2), a covalently linked antiparallel dimer of the MG2 analogue [(F5Y, L6C, F16W, I20C-MG2)(2): II] was synthesized based on the dimer structure revealed by our NMR study. The interactions of the dimer with lipid bilayers were investigated by CD and fluorescence in comparison with a monomer analogue (F5Y, F16W-MG2: I). Similar to I, II was found to form a peptide-lipid supramolecular complex pore accompanied with lipid flip-flop and peptide translocation. The pore formed by II was characterized by a slightly larger pore diameter and a threefold longer lifetime than that of I, although the pore formation rate of the dimer was lower than that of the monomer. The coexistence of the dimer and the monomer exhibited slight but significant synergism in membrane permeabilization, which was maximal at a monomer/dimer ratio of 3. Therefore, we concluded that a pentameric pore composed of one pore-stabilizing dimer and three monomers maximized the overall leakage activity in keeping with our kinetic prediction.
About this Structure
1DUM is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue., Hara T, Kodama H, Kondo M, Wakamatsu K, Takeda A, Tachi T, Matsuzaki K, Biopolymers. 2001 Apr 5;58(4):437-46. PMID:11180056 Page seeded by OCA on Fri May 2 14:17:41 2008
Categories: Single protein | Matsuzaki, K. | Tachi, T. | Takeda, A. | Wakamatsu, K. | Amphipathic helix | Antibiotic | Bilayer | Dimer | Magainin | Membrane | Vesicle
