1d9j: Difference between revisions
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==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE== | ==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE== | ||
<StructureSection load='1d9j' size='340' side='right' caption='[[1d9j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1d9j' size='340' side='right' caption='[[1d9j]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d9l|1d9l]], [[1d9m|1d9m]], [[1d9o|1d9o]], [[1d9p|1d9p]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d9l|1d9l]], [[1d9m|1d9m]], [[1d9o|1d9o]], [[1d9p|1d9p]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9j OCA], [http://pdbe.org/1d9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d9j RCSB], [http://www.ebi.ac.uk/pdbsum/1d9j PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9j OCA], [http://pdbe.org/1d9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d9j RCSB], [http://www.ebi.ac.uk/pdbsum/1d9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1d9j" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1d9j" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Magainin 2|Magainin 2]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:08, 30 August 2017
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
Function[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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