ArticleScientific reports2017
Arginase Structure and Inhibition: Catalytic Site Plasticity Reveals New Modulation Possibilities.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 44 citations in OpenAlex.
- Article
- The roles of arginases and arginine in immunity.Nature reviews. Immunology · 2025Review
- Derivatization of Microcystins Can Increase Target Inhibition while Reducing Cellular Uptake.Journal of natural products · 2025Article
- Screening of antihyperglycemic and cytotoxic properties ofIn silico pharmacology · 2025Article
- Trace Elements in Medicinal Metallomics.Mini reviews in medicinal chemistry · 2025Review
- Mind the Gap-Deciphering GPCR Pharmacology Using 3D Pharmacophores and Artificial Intelligence.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Benzimidazole Derivatives as New and Selective Inhibitors of Arginase fromInternational journal of molecular sciences · 2021Article
- Recent Advances in In Silico Target Fishing.Molecules (Basel, Switzerland) · 2021Review
- Cryo-EM structures of inhibitory antibodies complexed with arginase 1 provide insight into mechanism of action.Communications biology · 2021Article
- Biased Ligands Differentially Shape the Conformation of the Extracellular Loop Region in 5-HTInternational journal of molecular sciences · 2020Article
- Arginase as a Potential Biomarker of Disease Progression: A Molecular Imaging Perspective.International journal of molecular sciences · 2020Review
- Catching a Moving Target: Comparative Modeling of Flaviviral NS2B-NS3 Reveals Small Molecule Zika Protease Inhibitors.ACS medicinal chemistry letters · 2020Article
- Truly Target-Focused Pharmacophore Modeling: A Novel Tool for Mapping Intermolecular Surfaces.Molecules (Basel, Switzerland) · 2018Article
- Identifying medically relevant xenon protein targets byMedical gas researchArticle
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metalloenzyme arginase is a therapeutically relevant target associated with tumor growth. To fight cancer immunosuppression, arginase activity can be modulated by small chemical inhibitors binding to its catalytic center. To better understand molecular mechanisms of arginase inhibition, a careful computer-aided mechanistic structural investigation of this enzyme was conducted. Using molecular dynamics (MD) simulations in the microsecond range, key regions of the protein active site were identified and their flexibility was evaluated and compared. A cavity opening phenomenon was observed, involving three loops directly interacting with all known ligands, while metal coordinating regions remained motionless. A novel dynamic 3D pharmacophore analysis method termed dynophores has been developed that allows for the construction of a single 3D-model comprising all ligand-enzyme interactions occurring throughout a complete MD trajectory. This new technique for the in silico study of intermolecular interactions allows for loop flexibility analysis coupled with movements and conformational changes of bound ligands. Presented MD studies highlight the plasticity of the size of the arginase active site, leading to the hypothesis that larger ligands can enter the cavity of arginase. Experimental testing of a targeted fragment library substituted by different aliphatic groups validates this hypothesis, paving the way for the design of arginase inhibitors with novel binding patterns.
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Registered trials
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