ArticleBiophysical journal2008
Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed.
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- Profiling Novel Quinuclidine-Based Derivatives as Potential Anticholinesterase Drugs: Enzyme Inhibition and Effects on Cell Viability.International journal of molecular sciences · 2023Article
- Design of electron-donating group substituted 2-PAM analogs as antidotes for organophosphate insecticide poisoning.RSC advances · 2023Article
- Engineering gain-of-function mutants of a WW domain by dynamics and structural analysis.Protein science : a publication of the Protein Society · 2023Article
- Structural and dynamic effects of paraoxon binding to human acetylcholinesterase by X-ray crystallography and inelastic neutron scattering.Structure (London, England : 1993) · 2022Article
- Potential of Vitamin B6 Dioxime Analogues to Act as Cholinesterase Ligands.International journal of molecular sciences · 2022Article
- 4-Aminoquinoline-Based Adamantanes as Potential Anticholinesterase Agents in Symptomatic Treatment of Alzheimer's Disease.Pharmaceutics · 2022Article
- Chalcone Scaffolds Exhibiting Acetylcholinesterase Enzyme Inhibition: Mechanistic and Computational Investigations.Molecules (Basel, Switzerland) · 2022Article
- Chemical Composition and Preliminary Toxicity Evaluation of the Essential Oil fromMolecules (Basel, Switzerland) · 2021Article
- A Comprehensive Review of Cholinesterase Modeling and Simulation.Biomolecules · 2021Review
- Essential Oils as a Potential Neuroprotective Remedy for Age-Related Neurodegenerative Diseases: A Review.Molecules (Basel, Switzerland) · 2021Review
- Structure-Based Scaffold Repurposing toward the Discovery of Novel Cholinesterase Inhibitors.ACS omega · 2020Article
- Vitamin B3-Based Biologically Active Compounds as Inhibitors of Human Cholinesterases.International journal of molecular sciences · 2020Article
- Three-Component Access to Functionalized Spiropyrrolidine Heterocyclic Scaffolds and Their Cholinesterase Inhibitory Activity.Molecules (Basel, Switzerland) · 2020Article
- Molecular docking analysis of HER-2 inhibitor from the ZINC database as anticancer agents.Bioinformation · 2020Article
- Synthesis of novel vanillin derivatives: novel multi-targeted scaffold ligands against Alzheimer's disease.MedChemComm · 2019Article
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7 authors.
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Abstract
The high aromatic content of the deep and narrow active-site gorge of acetylcholinesterase (AChE) is a remarkable feature of this enzyme. Here, we analyze conformational flexibility of the side chains of the 14 conserved aromatic residues in the active-site gorge of Torpedo californica AChE based on the 47 three-dimensional crystal structures available for the native enzyme, and for its complexes and conjugates, and on a 20-ns molecular dynamics (MD) trajectory of the native enzyme. The degree of flexibility of these 14 aromatic side chains is diverse. Although the side-chain conformations of F330 and W279 are both very flexible, the side-chain conformations of F120, W233, W432, Y70, Y121, F288, F290 and F331 appear to be fixed. Residues located on, or adjacent to, the Omega-loop (C67-C94), namely W84, Y130, Y442, and Y334, display different flexibilities in the MD simulations and in the crystal structures. An important outcome of our study is that the majority of the side-chain conformations observed in the 47 Torpedo californica AChE crystal structures are faithfully reproduced by the MD simulation on the native enzyme. Thus, the protein can assume these conformations even in the absence of the ligand that permitted their experimental detection. These observations are pertinent to structure-based drug design.
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