1dum: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (13 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES== | ||
<StructureSection load='1dum' size='340' side='right'caption='[[1dum]]' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<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> | |||
</table> | |||
== Function == | |||
[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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dum" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Magainin 2|Magainin 2]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Xenopus laevis]] | |||
[[Category: Matsuzaki K]] | |||
[[Category: Tachi T]] | |||
[[Category: Takeda A]] | |||
[[Category: Wakamatsu K]] | |||
Latest revision as of 10:10, 9 August 2023
NMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLESNMR STRUCTURE OF [F5Y, F16W] MAGAININ 2 BOUND TO PHOSPHOLIPID VESICLES
Structural highlights
FunctionMAGA_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. Publication Abstract from PubMedTo 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||