Title : Limitations in current acetylcholinesterase structure-based design of oxime antidotes for organophosphate poisoning.

Pub. Date : 2016 Aug

PMID : 27371941






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Catalytically inactive OP-AChE conjugates formed between the active-center serine and phosphorus of OPs can, in principle, be reactivated by nucleophilic oxime antidotes. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens
2 Antidote efficacy is limited by the structural diversity of OP-AChE conjugates resulting from differences in the structure of the conjugated OP, the different active-center volumes they occupy when conjugated to the active-center serine of AChE, and the distinct chemical characteristics of both OPs and oximes documented in numerous X-ray structures of OP-conjugated AChEs. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens
3 Antidote efficacy is limited by the structural diversity of OP-AChE conjugates resulting from differences in the structure of the conjugated OP, the different active-center volumes they occupy when conjugated to the active-center serine of AChE, and the distinct chemical characteristics of both OPs and oximes documented in numerous X-ray structures of OP-conjugated AChEs. Serine acetylcholinesterase (Cartwright blood group) Homo sapiens