Title : Structures of human acetylcholinesterase in complex with pharmacologically important ligands - Cheung_2012_J.Med.Chem_55_10282 |
Author(s) : Cheung J , Rudolph MJ , Burshteyn F , Cassidy MS , Gary EN , Love J , Franklin MC , Height JJ |
Ref : Journal of Medicinal Chemistry , 55 :10282 , 2012 |
Abstract :
Human acetylcholinesterase (AChE) is a significant target for therapeutic drugs. Here we present high resolution crystal structures of human AChE, alone and in complexes with drug ligands; donepezil, an Alzheimer's disease drug, binds differently to human AChE than it does to Torpedo AChE. These crystals of human AChE provide a more accurate platform for further drug development than previously available. |
PubMedSearch : Cheung_2012_J.Med.Chem_55_10282 |
PubMedID: 23035744 |
Gene_locus related to this paper: human-ACHE |
Inhibitor | Aricept~Donepezil~E2020 Fasciculin2 Galanthamine HuperzineA |
Gene_locus | human-ACHE |
Structure | 4EY4 4EY5 4EY6 4EY7 4EY8 |
Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ (2012)
Structures of human acetylcholinesterase in complex with pharmacologically important ligands
Journal of Medicinal Chemistry
55 :10282
Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ (2012)
Journal of Medicinal Chemistry
55 :10282