4EY5

Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A

Summary for 4EY5

• Entry DOI: 10.2210/pdb4ey5/pdb
• Descriptor: Acetylcholinesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, Huperzine A, ... (8 entities in total)
• Functional Keywords: acetylcholinesterase, hydrolase, huperzine a, inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 121207.61

Authors

Cheung, J.,Rudolph, M.,Burshteyn, F.,Cassidy, M.,Gary, E.,Love, J.,Height, J.,Franklin, M. (deposition date: 2012-05-01, release date: 2012-10-17, Last modification date: 2024-11-06)

Primary citation

Cheung, J.,Rudolph, M.J.,Burshteyn, F.,Cassidy, M.S.,Gary, E.N.,Love, J.,Franklin, M.C.,Height, J.J.
Structures of human acetylcholinesterase in complex with pharmacologically important ligands.
J.Med.Chem., 55:10282-10286, 2012

PubMed 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.

PubMed: 23035744
DOI: 10.1021/jm300871x

Experimental method

X-RAY DIFFRACTION (2.3012 Å)