1D9O
SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P3)
Summary for 1D9O
| Entry DOI | 10.2210/pdb1d9o/pdb |
| Related | 1D9J 1D9L 1D9M 1D9P |
| Descriptor | CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE (1 entity in total) |
| Functional Keywords | random-hinge-helix, membrane protein |
| Biological source | Xenopus laevis, Hyalophora cecropia (African clawed frog, cecropia moth) |
| Total number of polymer chains | 1 |
| Total formula weight | 2295.92 |
| Authors | |
| Primary citation | Oh, D.,Shin, S.Y.,Kang, J.H.,Hahm, K.S.,Kim, K.L.,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., 53:578-589, 1999 Cited by PubMed Abstract: 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. PubMed: 10424354DOI: 10.1034/j.1399-3011.1999.00067.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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