Detailed Information on Publication Record
2005
Structure and dynamics of sarin-inhibited acetylcholinesterase
WIESNER, Jiří, Zdeněk KŘÍŽ and Jaroslav KOČABasic information
Original name
Structure and dynamics of sarin-inhibited acetylcholinesterase
Name in Czech
Struktura a dynamika acetylcholinesterázy inhibované sarinem
Authors
WIESNER, Jiří (203 Czech Republic, guarantor), Zdeněk KŘÍŽ (203 Czech Republic) and Jaroslav KOČA (203 Czech Republic)
Edition
Praha, Modeling Interactions in Biomolecules II, p. 1-1, 1 pp. 2005
Publisher
Univerzita Karlova, Praha
Other information
Language
English
Type of outcome
Stať ve sborníku
Field of Study
10403 Physical chemistry
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14330/05:00013282
Organization unit
Faculty of Informatics
Keywords in English
computational chemistry;computer modeling;molecular dynamics;MD;acetycholinesterase;AChE;nerve agent;irreversible inhibition;sarin
Tags
Změněno: 27/4/2006 20:08, RNDr. JUDr. Vladimír Šmíd, CSc.
V originále
Serine protease acetylcholinesterase (AChE, EC 3.1.1.7) is one of the most crucial enzymes for nerve response and function. In cholinergic nervous system, AChE terminates transmission of neuronal impulses by catalysing the hydrolysis of neurotransmitter, acetylcholine. It is one of the most efficient enzymes ever known. Highly toxic organophosphorus compounds, such as sarin, soman or tabun (nerve agents), are able to inhibit AChE by phosphonylation of its active site serine. Severe nerve agent intoxication leads to muscle spasms, cessation of breathing and instantaneous death. Structure of nerve agent inhibited AChE is not exactly known although one crystallographic structure (1SOM) of soman inhibited AChE was published. Thus a model of sarin inhibited mouse AChE was constructed and molecular dynamics was calculated to further characterize its properties. The explicit solvent molecular dynamics simulation under NPT conditions was performed by the Amber program suite. Simulation temperature was 300K and TIP3P water model was used. The stability of secondary structures and interactions of residues in AChE active site during molecular dynamics were analysed.
In Czech
Struktura a dynamika acetylcholinesterázy inhibované sarinem
Links
| GD204/03/H016, research and development project |
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| MSM0021622413, plan (intention) |
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