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    • A Single Nucleotide Polymorphism Translates into a Radical Amino Acid Substitution at the Ligand-Binding Site in Fasciola hepatica Carboxylesterase B 

      Miranda-Miranda, Estefan; Scarcella, Silvana; Reynaud, Enrique; Narváez-Padilla, Verónica; Neira, Gisela; Mera y Sierra, Roberto; Aguilar-Díaz, Hugo; Cossio-Bayugar, Raquel (Comite editorial GENES, 2022-10-19)
      Fasciola hepatica anthelmintic resistance may be associated with the catalytic activity of xenobiotic metabolizing enzymes. The gene expression of one of these enzymes, identified as car boxylesterase B (CestB), was previously described as inducible in adult parasites under anthelmintic treatment and exhibited a single nucleotide polymorphism at position 643 that translates into a radical amino acid substitution at position 215 from Glutamic acid to Lysine. Alphafold 3D models of both allelic sequences exhibited a significant affinity pocket rearrangement and different ligand-docking modeling ...