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1d9o

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[[Image:1d9o.png|left|200px]]
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==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P3)==
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<StructureSection load='1d9o' size='340' side='right' caption='[[1d9o]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d9o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D9O FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d9j|1d9j]], [[1d9l|1d9l]], [[1d9m|1d9m]], [[1d9p|1d9p]]</td></tr>
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<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=1d9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1d9o RCSB], [http://www.ebi.ac.uk/pdbsum/1d9o 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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In order to elucidate the structure-antibiotic activity relationships of the peptides, the three-dimensional structures of two hybrid peptides, CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) in trifluoroethanol-containing aqueous solution were investigated by NMR spectroscopy. Both CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) have strong antibacterial activity but only CA(1-8) - ME(1-12) has hemolytic activity against human erythrocytes. CA(1-8) - MA(1-12) has a hydrophobic 310-helix of only two turns combined with one short helix in the N-terminus with a flexible hinge section in between. CA(1-8) - MA(1-12) has a severely bent structure in the middle of the peptide. These structural features as well as the low hydrophobicity of CA(1-8) - MA(1-12) seem to be crucial for the selective lysis against the membrane of prokaryotic cells. CA(1-8) - ME(1-12) has an alpha-helical structure of about three turns in the melittin domain and a flexible structure with one turn in the cecropin domain connected with a flexible hinge section in between, and these might be the structural features required for membrane disruption against prokaryotic and eukaryotic cells. The central hinge region (Gly9-Ile10-Gly11) in an amphipathic antibacterial peptide is considered to play an important role in providing the conformational flexibility required for ion channel formation of the C-terminal hydrophobic alpha-helix on cell membrane.
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{{STRUCTURE_1d9o| PDB=1d9o | SCENE= }}
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NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptides.,Oh D, Shin SY, Kang JH, Hahm KS, Kim KL, Kim Y J Pept Res. 1999 May;53(5):578-89. PMID:10424354<ref>PMID:10424354</ref>
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===SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P3)===
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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_10424354}}
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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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[[1d9o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9O OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:010424354</ref><references group="xtra"/>
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[[Category: Hyalophora cecropia]]
[[Category: Hyalophora cecropia]]
[[Category: Kim, Y.]]
[[Category: Kim, Y.]]

Revision as of 06:30, 4 September 2014

SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P3)

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