ArticleProtein science : a publication of the Protein Society1996
Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 61 citations in OpenAlex.
- Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.Molecules (Basel, Switzerland) · 2017Review
- A novel role for synaptic acetylcholinesterase as an apoptotic deoxyribonuclease.Cell discovery · 2015Article
- Structural insights into antibody sequestering and neutralizing of Na+ channel α-type modulator from old world scorpion venom.The Journal of biological chemistry · 2012Article
- Naturally occurring variations in the human cholinesterase genes: heritability and association with cardiovascular and metabolic traits.The Journal of pharmacology and experimental therapeutics · 2011Article
- Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state.Journal of the American Chemical Society · 2010Article
- Homology modelling and spectroscopy, a never-ending love story.European biophysics journal : EBJ · 2010Review
- Inactivation of acetylcholinesterase by various fluorophores.Journal of enzyme inhibition and medicinal chemistry · 2010Article
- Article
- Plant-derived human acetylcholinesterase-R provides protection from lethal organophosphate poisoning and its chronic aftermath.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2007Article
- A server and database for dipole moments of proteins.Nucleic acids research · 2007Article
- Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering.Structure (London, England : 1993) · 2007Article
- Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors.The EMBO journal · 2005Article
- Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates.The Biochemical journal · 2003Article
- Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.The EMBO journal · 2003Article
- Tetramerization domain of human butyrylcholinesterase is at the C-terminus.The Biochemical journal · 1997Article
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
Abstract
A soluble, monomeric form of acetylcholinesterase from mouse (mAChE), truncated at its carboxyl-terminal end, was generated from a cDNA encoding the glycophospholipid-linked form of the mouse enzyme by insertion of an early stop codon at position 549. Insertion of the cDNA behind a cytomegalovirus promoter and selection by aminoglycoside resistance in transfected HEK cells yielded clones secreting large quantities of mAChE into the medium. The enzyme sediments as a soluble monomer at 4.8 S. High levels of expression coupled with a one-step purification by affinity chromatography have allowed us to undertake a crystallographic study of the fasciculin-mAChE complex. Complexes of two distinct fasciculins, Fas1-mAChE and Fas2-mAChE, were formed prior to the crystallization and were characterized thoroughly. Single hexagonal crystals, up to 0.6 mm x 0.5 mm x 0.5 mm, grew spontaneously from ammonium sulfate solutions buffered in the pH 7.0 range. They were found by electrophoretic migration to consist entirely of the complex and diffracted to 2.8 A resolution. Analysis of initial X-ray data collected on Fas2-mAChE crystals identified the space group as P6(1)22 or P6(5)22 with unit cell dimensions a = b = 75.5 A, c = 556 A, giving a Vm value of 3.1 A3/Da (or 60% of solvent), consistent with a single molecule of Fas2-AChE complex (72 kDa) per asymmetric unit. The complex Fas1-mAChE crystallizes in the same space group with identical cell dimensions.
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