2otq: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1qvk|1QVK]], [[1qvl|1QVL]], [[1ski|1SKI]], [[1skk|1SKK]], [[1skl|1SKL]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2otq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2otq OCA], [http://www.ebi.ac.uk/pdbsum/2otq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2otq RCSB]</span>
}}
}}


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[[Category: cationic antimicrobial peptide]]
[[Category: cationic antimicrobial peptide]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:04:20 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:22:59 2008''

Revision as of 01:23, 31 March 2008

File:2otq.jpg


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2otq
Related: 1QVK, 1QVL, 1SKI, 1SKK, 1SKL


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of the antimicrobial peptide cyclo(RRWFWR) bound to DPC micelles


Overview

New antimicrobial compounds are of major importance because of the growing problem of bacterial resistance. In this context, antimicrobial peptides have received a lot of attention. Their mechanism of action, however, is often obscure. Here, the structures of two cyclic, antimicrobial peptides from the family of arginine- and tryptophan-rich peptides determined in a membrane-mimicking environment are described. The sequence of the peptides has been obtained from a cyclic parent peptide by scrambling the amino acids. While the activity of the peptides is similar to that of the parent peptide, the structures are not. The peptides do, however, all adopt an amphiphilic structure. A comparison between the structures helps to define the requirements for the activity of these peptides. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.

About this Structure

2OTQ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Structures of cyclic, antimicrobial peptides in a membrane-mimicking environment define requirements for activity., Appelt C, Wessolowski A, Dathe M, Schmieder P, J Pept Sci. 2007 Nov 6;. PMID:17985394

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