1cz6

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cz6 OCA], [http://www.ebi.ac.uk/pdbsum/1cz6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cz6 RCSB]</span>
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[[Category: peptide]]
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Revision as of 16:31, 30 March 2008


PDB ID 1cz6

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



SOLUTION STRUCTURE OF ANDROCTONIN


Overview

Androctonin is a highly cationic antimicrobial peptide from scorpion exhibiting a broad spectrum of activities against bacteria and fungi. It contains 25 amino acids including four cysteine residues forming two disulfide bridges. We report here on the determination of its solution structure by conventional two-dimensional (2D) 1H-NMR spectroscopy and molecular modelling using distance geometry and molecular dynamics methods. The structure of androctonin involves a well-defined highly twisted anti-parallel beta-sheet with strands connected by a more variable positively charged turn. A comparison with the structure of tachyplesin I (horseshoe crab) reveals that the amphiphilic character of the protein surface of this homologous peptide is not observed in androctonin. We have undertaken a 200-ps molecular dynamics simulation study on a system including one androctonin molecule and a monolayer of DMPG (1,2-dimyristoylphosphatidylglycerol) lipids. On the basis of this simulation, the first steps of the membrane permeabilization process are discussed.

About this Structure

1CZ6 is a Single protein structure of sequence from Androctonus australis. Full crystallographic information is available from OCA.

Reference

Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer., Mandard N, Sy D, Maufrais C, Bonmatin JM, Bulet P, Hetru C, Vovelle F, J Biomol Struct Dyn. 1999 Oct;17(2):367-80. PMID:10563585

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