1cz6
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(New page: 200px<br /><applet load="1cz6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cz6" /> '''SOLUTION STRUCTURE OF ANDROCTONIN'''<br /> ...)
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Revision as of 10:45, 20 November 2007
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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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