1dum: Difference between revisions

Revision as of 11:44, 20 March 2008

Coordinates:

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

OverviewOverview

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 StructureAbout this Structure

1DUM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Mar 20 10:44:37 2008

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OCA

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-[[Image:1dum.gif|left|200px]]<br /><applet load="1dum" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dum.gif|left|200px]]
-caption="1dum" />
-'''NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES'''<br />
+ {{Structure
+|PDB= 1dum |SIZE=350|CAPTION= <scene name='initialview01'>1dum</scene>
+|SITE=
+|LIGAND=
+|ACTIVITY=
+|GENE=
+}}
+'''NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-DUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA].
+DUM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11180056 11180056]
+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]
 [[Category: Single protein]]
 [[Category: Matsuzaki, K.]]
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 [[Category: vesicle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:37 2008''