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Structure of acetylcholinesterase complexed with the nootropic alkaloid, (–)-huperzine A

✍ Scribed by Raves, Mia L. ;Harel, Michal ;Pang, Yuan-Ping ;Silman, Israel ;Kozikowski, Alan P. ;Sussman, Joel L.


Book ID
109964497
Publisher
Nature Publishing Group
Year
1997
Tongue
English
Weight
825 KB
Volume
4
Category
Article
ISSN
1545-9993

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Two molecular dynamics simulations were performed for a modeled complex of mouse acetylcholinesterase liganded with huperzine A (HupA). Analysis of these simulations shows that HupA shifts in the active site toward Tyr 337 and Phe 338, and that several residues in the active site area reach out to m

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A 1 ns molecular dynamics simulation of unliganded mouse acetylcholinesterase (AChE) is compared to a previous simulation of mouse AChE complexed with huperzine A (HupA). Several common features are observed. In both simulations, the active site gorge fluctuates in size during the 1 ns trajectory an