1cz6
From Proteopedia
(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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'''SOLUTION STRUCTURE OF ANDROCTONIN'''<br /> | '''SOLUTION STRUCTURE OF ANDROCTONIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Androctonin is a highly cationic antimicrobial peptide from scorpion | + | 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== | ==About this Structure== | ||
| - | 1CZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http:// | + | 1CZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZ6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peptide]] | [[Category: peptide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:15 2008'' |
Revision as of 10:11, 21 February 2008
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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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