1D9M

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

1D9M の概要

• エントリーDOI: 10.2210/pdb1d9m/pdb
• 関連するPDBエントリー: 1D9J 1D9L 1D9O 1D9P
• 分子名称: CECROPIN A(1-8)-MAGAININ 2 HYBRID PEPTIDE ANALOGUE (1 entity in total)
• 機能のキーワード: helix-hinge-helix, membrane protein
• 由来する生物種: Xenopus laevis, Hyalophora cecropia (African clawed frog, cecropia moth)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2280.90

構造登録者

Oh, D.,Kim, Y. (登録日: 1999-10-28, 公開日: 1999-11-12, 最終更新日: 2024-11-20)

主引用文献

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

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: 10424354
DOI: 10.1034/j.1399-3011.1999.00067.x

実験手法

SOLUTION NMR