1dum

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[[Image:1dum.gif|left|200px]]
 
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==NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES==
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The line below this paragraph, containing "STRUCTURE_1dum", creates the "Structure Box" on the page.
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<StructureSection load='1dum' size='340' side='right'caption='[[1dum]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1dum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1DUM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dum OCA], [https://pdbe.org/1dum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dum RCSB], [https://www.ebi.ac.uk/pdbsum/1dum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dum ProSAT]</span></td></tr>
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{{STRUCTURE_1dum| PDB=1dum | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAGA_XENLA MAGA_XENLA] Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.
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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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'''NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES'''
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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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==Overview==
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1DUM is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA].
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</div>
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<div class="pdbe-citations 1dum" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11180056 11180056]
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*[[Magainin 2|Magainin 2]]
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[[Category: Single protein]]
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== References ==
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[[Category: Matsuzaki, K.]]
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<references/>
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[[Category: Tachi, T.]]
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__TOC__
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[[Category: Takeda, A.]]
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</StructureSection>
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[[Category: Wakamatsu, K.]]
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[[Category: Large Structures]]
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[[Category: Amphipathic helix]]
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[[Category: Xenopus laevis]]
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[[Category: Antibiotic]]
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[[Category: Matsuzaki K]]
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[[Category: Bilayer]]
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[[Category: Tachi T]]
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[[Category: Dimer]]
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[[Category: Takeda A]]
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[[Category: Magainin]]
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[[Category: Wakamatsu K]]
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[[Category: Membrane]]
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[[Category: Vesicle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:17:41 2008''
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Current revision

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

PDB ID 1dum

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