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Structures of Human Acetylcholinesterase in Complex with Pharmacologically Important Ligands

Journal of Medicinal Chemistry · 2012 · Vol. 55(22) · pp. 10282–10286

Jonah Cheung✉(New York Structural Biology Center)M. Rudolph(New York Structural Biology Center)F. Burshteyn(New York Structural Biology Center)M. Cassidy(New York Structural Biology Center)E. Gary(New York Structural Biology Center)J. Love(New York Structural Biology Center)Matthew C. Franklin(New York Structural Biology Center)J.J. Height(U.S. Army Combat Capabilities Development Command Chemical Biological Center)

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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.

Cholinesterase and Neurodegenerative Diseases Computational Drug Discovery Methods Enzyme function and inhibitionAcetylcholinesteraseChemistryDonepezilAchéTorpedoDrugPharmacologyEnzymeStereochemistryBiochemistry

MeSH terms

DonepezilAcetylcholinesteraseAcetylthiocholineAnimalsCholinesterase InhibitorsHumansIndansModels, MolecularPiperidinesProtein ConformationTorpedoCrystallography, X-Ray

Funding

U.S. Department of Defense
U.S. Department of Energy
Office of Science
Basic Energy Sciences
Edgewood Chemical Biological Center

Citations

1,291

FWCI

19.48

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100%

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References

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

Protein Science · 1993 · 570 citations

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