1d9p: Difference between revisions
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'''SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P4)''' | {{Structure | ||
|PDB= 1d9p |SIZE=350|CAPTION= <scene name='initialview01'>1d9p</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P4)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1D9P is a [ | 1D9P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis_+_hyalophora_cecropia Xenopus laevis + hyalophora cecropia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9P OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10424354 10424354] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis + hyalophora cecropia]] | [[Category: Xenopus laevis + hyalophora cecropia]] | ||
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[[Category: helix-hinge-helix]] | [[Category: helix-hinge-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:35:02 2008'' | ||
Revision as of 11:35, 20 March 2008
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SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P4)
OverviewOverview
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.
About this StructureAbout this Structure
1D9P is a Single protein structure of sequence from Xenopus laevis + hyalophora cecropia. Full crystallographic information is available from OCA.
ReferenceReference
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
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