1dum

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[[Image:1dum.png|left|200px]]
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==NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES==
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<StructureSection load='1dum' size='340' side='right' caption='[[1dum]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dum]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DUM FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dum OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dum RCSB], [http://www.ebi.ac.uk/pdbsum/1dum PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1dum| PDB=1dum | SCENE= }}
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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<ref>PMID:11180056</ref>
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===NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_11180056}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1dum]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA].
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</StructureSection>
[[Category: Matsuzaki, K.]]
[[Category: Matsuzaki, K.]]
[[Category: Tachi, T.]]
[[Category: Tachi, T.]]

Revision as of 10:50, 10 September 2014

NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES

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