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PDBsum entry 1d9m
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Membrane protein PDB id
1d9m

 

 

 

 

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Contents
Protein chain
19 a.a.
PDB id:
1d9m
Name: Membrane protein
Title: Solution structure of cecropin a(1-8)-magainin 2 hybrid peptide analogue(p2)
Structure: Cecropin a(1-8)-magainin 2 hybrid peptide analogue. Chain: a. Engineered: yes
Source: Xenopus laevis, hyalophora cecropia. African clawed frog, cecropia moth. Organism_taxid: 8355,7123. Strain: ,. Cellular_location: membrane
NMR struc: 20 models
Authors: D.Oh,Y.Kim
Key ref: D.Oh et al. (1999). 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. PubMed id: 10424354
Date:
28-Oct-99     Release date:   12-Nov-99    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01507  (CECA_HYACE) -  Cecropin-A from Hyalophora cecropia
Seq:
Struc: 		64 a.a.
19 a.a.*
Protein chain
P11006  (MAGA_XENLA) -  Magainins from Xenopus laevis
Seq:
Struc: 		303 a.a.
19 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 19 residue positions (black crosses)

 

 
J Pept Res 53:578-589 (1999)
PubMed id: 10424354  
 
 
NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptides.
D.Oh, S.Y.Shin, J.H.Kang, K.S.Hahm, K.L.Kim, Y.Kim.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21053260 M.Gupta, and V.S.Chauhan (2011).
De novo design of α,β-didehydrophenylalanine containing peptides: From models to applications.
  Biopolymers, 95, 161-173.  
19957017 W.Huang, L.Lu, X.Shao, C.Tang, and X.Zhao (2010).
Anti-melanoma activity of hybrid peptide P18 and its mechanism of action.
  Biotechnol Lett, 32, 463-469.  
18078805 D.W.Hoskin, and A.Ramamoorthy (2008).
Studies on anticancer activities of antimicrobial peptides.
  Biochim Biophys Acta, 1778, 357-375.  
17394119 P.Mathur, N.R.Jagannathan, and V.S.Chauhan (2007).
Alpha,beta-dehydrophenylalanine containing cecropin-melittin hybrid peptides: conformation and activity.
  J Pept Sci, 13, 253-262.  
16170803 C.Landon, H.Meudal, N.Boulanger, P.Bulet, and F.Vovelle (2006).
Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an alpha-helical conformation.
  Biopolymers, 81, 92.
PDB codes: 1zrv 1zrw 1zrx
16880985 V.M.Bhor, C.J.Thomas, N.Surolia, and A.Surolia (2005).
Polymyxin B: an ode to an old antidote for endotoxic shock.
  Mol Biosyst, 1, 213-222.  
11906604 Y.Chen, C.T.Mant, and R.S.Hodges (2002).
Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix.
  J Pept Res, 59, 18-33.  
11009597 D.Oh, S.Y.Shin, S.Lee, J.H.Kang, S.D.Kim, P.D.Ryu, K.S.Hahm, and Y.Kim (2000).
Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures.
  Biochemistry, 39, 11855-11864.
PDB codes: 1f0d 1f0e 1f0f 1f0g 1f0h
10651822 V.Frecer, B.Ho, and J.L.Ding (2000).
Interpretation of biological activity data of bacterial endotoxins by simple molecular models of mechanism of action.
  Eur J Biochem, 267, 837-852.  
10590307 B.Bechinger (1999).
The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy.
  Biochim Biophys Acta, 1462, 157-183.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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