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| | ==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE(P2)== | | ==SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE(P2)== |
| - | <StructureSection load='1d9m' size='340' side='right' caption='[[1d9m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1d9m' size='340' side='right'caption='[[1d9m]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1d9m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D9M FirstGlance]. <br> | + | <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> |
| - | </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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d9j|1d9j]], [[1d9l|1d9l]], [[1d9o|1d9o]], [[1d9p|1d9p]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9m OCA], [http://pdbe.org/1d9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d9m RCSB], [http://www.ebi.ac.uk/pdbsum/1d9m PDBsum]</span></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=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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CECA_HYACE CECA_HYACE]] Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1d9m" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1d9m" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Magainin 2|Magainin 2]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: African clawed frog]] | + | [[Category: Hyalophora cecropia]] |
| - | [[Category: Kim, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Oh, D]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Helix-hinge-helix]] | + | [[Category: Kim Y]] |
| - | [[Category: Membrane protein]] | + | [[Category: Oh D]] |
| Structural highlights
Function
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.CECA_HYACE Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oh D, Shin SY, Kang JH, Hahm KS, Kim KL, Kim Y. NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptides. J Pept Res. 1999 May;53(5):578-89. PMID:10424354
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