1d9j: Difference between revisions
New page: left|200px<br /><applet load="1d9j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d9j" /> '''SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAIN... |
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== | ==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE== | ||
In order to elucidate the structure-antibiotic activity relationships of | <StructureSection load='1d9j' size='340' side='right'caption='[[1d9j]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1d9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9J FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9j OCA], [https://pdbe.org/1d9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9j RCSB], [https://www.ebi.ac.uk/pdbsum/1d9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9j 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.[https://www.uniprot.org/uniprot/CECA_HYACE CECA_HYACE] Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1d9j" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Magainin 2|Magainin 2]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hyalophora cecropia]] | |||
[[Category: Large Structures]] | |||
[[Category: Kim Y]] | |||
[[Category: Oh D]] | |||
Latest revision as of 09:31, 30 October 2024
SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDESOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE
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.CECA_HYACE Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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