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Journal of Medicinal Chemistry· 2012Q1

Structures of Human Acetylcholinesterase in Complex with Pharmacologically Important Ligands

Jonah Cheung, M. Rudolph, F. Burshteyn, M. Cassidy et al.

Short summary

High-resolution crystal structures of human acetylcholinesterase (AChE) reveal that the Alzheimer's drug donepezil binds differently to human AChE than to Torpedo AChE.

AI-generated from the title and abstract; the full text is not read.

Key points

  • High-resolution crystal structures of human acetylcholinesterase (AChE) were obtained.
  • Structures include AChE alone and in complex with drug ligands like donepezil.
  • Donepezil binds differently to human AChE than to Torpedo AChE.
  • These structures provide a more accurate platform for drug development.

AI-generated from the title and abstract; the full text is not read.

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.

The authors' abstract, as published at the source. Journal of Medicinal Chemistry, 2012 · DOI ↗

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Field: Pharmacology (Medicine)

PharmacologyMedicine