Influence of the Acetylcholinesterase Active Site Protonation on Omega Loop and Active Site Dynamics

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F10%3A00040921" target="_blank" >RIV/00216224:14310/10:00040921 - isvavai.cz</a>
Alternative codes found
RIV/60162694:G44__/10:00002356
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Influence of the Acetylcholinesterase Active Site Protonation on Omega Loop and Active Site Dynamics
Original language description
Existence of alternative entrances in acetylcholinesterase (AChE) could explain the contrast between the very high AChE catalytic efficiency and the narrow and long access path to the active site revealed by X-ray crystallography. Alternative entrances could facilitate diffusion of the reaction products or at least water and ions from the active site. Previous molecular dynamics simulations identified side door and back door as the most probable alternative entrances. The simulations of non-inhibited AChE suggested that the back door opening events occur only rarely (0.8% of the time in the 10ns trajectory). Here we present a molecular dynamics simulation of non-inhibited AChE, where the back door opening appears much more often (14% of the time in the12ns trajectory) and where the side door opening was observed quite frequently (78% of trajectory time).
Czech name
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Czech description
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP) Z - Vyzkumny zamer (s odkazem do CEZ) S - Specificky vyzkum na vysokych skolach V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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