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1d9m

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[[Image:1d9m.jpg|left|200px]]
 
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==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE(P2)==
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The line below this paragraph, containing "STRUCTURE_1d9m", creates the "Structure Box" on the page.
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<StructureSection load='1d9m' size='340' side='right'caption='[[1d9m]]' 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'>[[1d9m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9M FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_1d9m| PDB=1d9m | SCENE= }}
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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=1d9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9m OCA], [https://pdbe.org/1d9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9m RCSB], [https://www.ebi.ac.uk/pdbsum/1d9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9m ProSAT]</span></td></tr>
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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.[https://www.uniprot.org/uniprot/CECA_HYACE CECA_HYACE] Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
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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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'''SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE(P2)'''
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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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==Overview==
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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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==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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1D9M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis_+_hyalophora_cecropia Xenopus laevis + hyalophora cecropia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9M OCA].
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</div>
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<div class="pdbe-citations 1d9m" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10424354 10424354]
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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: Xenopus laevis + hyalophora cecropia]]
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<references/>
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[[Category: Kim, Y.]]
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__TOC__
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[[Category: Oh, D.]]
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</StructureSection>
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[[Category: Helix-hinge-helix]]
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[[Category: Hyalophora cecropia]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:36:15 2008''
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[[Category: Large Structures]]
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[[Category: Xenopus laevis]]
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[[Category: Kim Y]]
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[[Category: Oh D]]

Current revision

SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE(P2)

PDB ID 1d9m

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