Structure and dynamics of sarin-inhibited acetylcholinesterase

D 2005

Structure and dynamics of sarin-inhibited acetylcholinesterase

WIESNER, Jiří, Zdeněk KŘÍŽ a Jaroslav KOČA

Základní údaje

Originální název

Structure and dynamics of sarin-inhibited acetylcholinesterase

Název česky

Struktura a dynamika acetylcholinesterázy inhibované sarinem

Autoři

WIESNER, Jiří (203 Česká republika, garant), Zdeněk KŘÍŽ (203 Česká republika) a Jaroslav KOČA (203 Česká republika)

Vydání

Brno, Strukturní biofyzika makromolekul, od s. 21-21, 1 s. 2005

Nakladatel

Biofyzikálny ústav AVČR a MU v Brne

Další údaje

Jazyk

angličtina

Typ výsledku

Stať ve sborníku

Obor

10403 Physical chemistry

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14330/05:00013286

Organizační jednotka

Fakulta informatiky

Klíčová slova anglicky

computational chemistry;computer modeling;molecular dynamics;MD;acetycholinesterase;AChE;nerve agent;irreversible inhibition;sarin

Štítky

acetycholinesterase, AChE, computational chemistry, computer modeling, irreversible inhibition, MD, molecular dynamics, nerve agent, sarin

Změněno: 27. 4. 2006 20:09, RNDr. JUDr. Vladimír Šmíd, CSc.

Anotace

ORIG CZ

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.

Česky

Struktura a dynamika acetylcholinesterázy inhibované sarinem

Návaznosti

GD204/03/H016, projekt VaV

Název: Strukturní biofyzika makromolekul

Investor: Grantová agentura ČR, Strukturní biofyzika makromolekul

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

WIESNER, Jiří, Zdeněk KŘÍŽ a Jaroslav KOČA. Structure and dynamics of sarin-inhibited acetylcholinesterase. In Strukturní biofyzika makromolekul. Brno: Biofyzikálny ústav AVČR a MU v Brne, 2005, s. 21-21.

@inproceedings{629785,
   author = {Wiesner, Jiří and Kříž, Zdeněk and Koča, Jaroslav},
   address = {Brno},
   booktitle = {Strukturní biofyzika makromolekul},
   keywords = {computational chemistry;computer modeling;molecular dynamics;MD;acetycholinesterase;AChE;nerve agent;irreversible inhibition;sarin},
   language = {eng},
   location = {Brno},
   pages = {21-21},
   publisher = {Biofyzikálny ústav AVČR a MU v Brne},
   title = {Structure and dynamics of sarin-inhibited acetylcholinesterase},
   year = {2005}
}

TY  - JOUR
ID  - 629785
AU  - Wiesner, Jiří - Kříž, Zdeněk - Koča, Jaroslav
PY  - 2005
TI  - Structure and dynamics of sarin-inhibited acetylcholinesterase
PB  - Biofyzikálny ústav AVČR a MU v Brne
CY  - Brno
KW  - computational chemistry;computer modeling;molecular dynamics;MD;acetycholinesterase;AChE;nerve agent;irreversible inhibition;sarin
N2  - 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.
ER  -

WIESNER, Jiří, Zdeněk KŘÍŽ a Jaroslav KOČA. Structure and dynamics of sarin-inhibited acetylcholinesterase. In \textit{Strukturní biofyzika makromolekul}. Brno: Biofyzikálny ústav AVČR a MU v Brne, 2005, s.~21-21.

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