1d9p
From Proteopedia
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|PDB= 1d9p |SIZE=350|CAPTION= <scene name='initialview01'>1d9p</scene> | |PDB= 1d9p |SIZE=350|CAPTION= <scene name='initialview01'>1d9p</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d9j|1D9J]], [[1d9l|1D9L]], [[1d9m|1D9M]], [[1d9o|1D9O]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9p OCA], [http://www.ebi.ac.uk/pdbsum/1d9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d9p RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Kim, Y.]] | [[Category: Kim, Y.]] | ||
[[Category: Oh, D.]] | [[Category: Oh, D.]] | ||
| - | [[Category: NH2]] | ||
[[Category: helix-hinge-helix]] | [[Category: helix-hinge-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:37:28 2008'' |
Revision as of 16:37, 30 March 2008
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| Ligands: | |||||||
| Related: | 1D9J, 1D9L, 1D9M, 1D9O
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF CECROPIN A(1-8)-MAGAININ 2(1-12) HYBRID PEPTIDE ANALOGUE(P4)
Overview
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 Structure
1D9P is a Single protein structure of sequence from Xenopus laevis + hyalophora cecropia. Full crystallographic information is available from OCA.
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:10424354
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