4ey8
From Proteopedia
Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2
Structural highlights
FunctionACES_HUMAN Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.[1] [2] [3] [4] Publication Abstract from PubMedHuman 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. Structures of human acetylcholinesterase in complex with pharmacologically important ligands.,Cheung J, Rudolph MJ, Burshteyn F, Cassidy MS, Gary EN, Love J, Franklin MC, Height JJ J Med Chem. 2012 Oct 4. PMID:23035744[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Dendroaspis angusticeps | Homo sapiens | Large Structures | Burshteyn F | Cassidy M | Cheung J | Franklin M | Gary E | Height J | Love J | Rudolph M