1dum: Difference between revisions

Revision as of 23:38, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dum.png

Template:STRUCTURE 1dum

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

Template:ABSTRACT PUBMED 11180056

About this StructureAbout this Structure

1DUM is a Single protein structure. Full experimental 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 Mon Jun 30 23:38:29 2008

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OCA

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-[[Image:1dum.gif|left|200px]]
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 {{STRUCTURE_1dum|  PDB=1dum  |  SCENE=  }}
-'''NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11180056}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11180056 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11180056}}
 ==About this Structure==
-DUM is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA].
+DUM is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUM OCA].
 ==Reference==
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 [[Category: Membrane]]
 [[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 Mon Jun 30 23:38:29 2008''