1d9m: Difference between revisions

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[[Image:1d9m.jpg|left|200px]]
{{Seed}}
[[Image:1d9m.png|left|200px]]


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{{STRUCTURE_1d9m|  PDB=1d9m  |  SCENE=  }}  
{{STRUCTURE_1d9m|  PDB=1d9m  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_10424354}}


==About this Structure==
==About this Structure==
1D9M 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=1D9M OCA].  
1D9M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis_+_hyalophora_cecropia Xenopus laevis + hyalophora cecropia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9M OCA].  


==Reference==
==Reference==
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[[Category: Oh, D.]]
[[Category: Oh, D.]]
[[Category: Helix-hinge-helix]]
[[Category: Helix-hinge-helix]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:36:15 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:42:43 2008''

Revision as of 19:42, 30 June 2008

File:1d9m.png

Template:STRUCTURE 1d9m

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

Template:ABSTRACT PUBMED 10424354

About this Structure

1D9M is a Single protein structure of sequence from Xenopus laevis + hyalophora cecropia. Full experimental 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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