Structures of human acetylcholinesterase in complex with pharmacologically important ligands

Jonah Cheung, Michael J. Rudolph, Fiana Burshteyn, Michael S. Cassidy, Ebony N. Gary, James Love, Matthew C. Franklin, Jude J. Height

Research output: Contribution to journalArticle

381 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)10282-10286
Number of pages5
JournalJournal of Medicinal Chemistry
Volume55
Issue number22
DOIs
StatePublished - Nov 26 2012

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ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

Cite this

Cheung, J., Rudolph, M. J., Burshteyn, F., Cassidy, M. S., Gary, E. N., Love, J., Franklin, M. C., & Height, J. J. (2012). Structures of human acetylcholinesterase in complex with pharmacologically important ligands. Journal of Medicinal Chemistry, 55(22), 10282-10286. https://doi.org/10.1021/jm300871x