Title : Mechanism of interaction of novel uncharged, centrally active reactivators with OP-hAChE conjugates.

Pub. Date : 2013 Mar 25

PMID : 22975155






1 Functional Relationships(s)
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1 Computational molecular modeling of RS41A and RS194B interactions with VX inhibited hAChE, bound reversibly in Michaelis type complex and covalently in the pentacoordinate reaction intermediate suggests that the faster reactivation reaction is a consequence of a tighter RS194B interactions with hAChE peripheral site (PAS) residues, in particular with D74, resulting in lower interaction energies for formation of both the binding and reactivation states. Aminosalicylic Acid acetylcholinesterase (Cartwright blood group) Homo sapiens