title: Probing the dimerization interface of Leishmania infantum trypanothione reductase with site-directed mutagenesis and short peptides.
abstract: Binding at the interface: We tested the inhibitory activity of a set of peptide sequences derived from an α-helix of the dimeric trypanothione reductase from Leishmania infantum. Replacement of a glutamic acid residue with a lysine promoted monomer dissociation and enzyme inhibition.
authors.affiliation: Departamento de Biología de Sistemas, Unidad Asociada de I+D+I al CSIC, Universidad de Alcalá, 28871 Alcalá de Henares, Madrid, Spain.
authors.forename: Miguel A
authors.initials: MA
authors.lastname: Toro
authors.forename: Pedro A
authors.initials: PA
authors.lastname: Sánchez-Murcia
authors.forename: David
authors.initials: D
authors.lastname: Moreno
authors.forename: Marta
authors.initials: M
authors.lastname: Ruiz-Santaquiteria
authors.forename: Juan Fernando
authors.initials: JF
authors.lastname: Alzate
authors.forename: Ana
authors.initials: A
authors.lastname: Negri
authors.forename: María-José
authors.initials: MJ
authors.lastname: Camarasa
authors.forename: Federico
authors.initials: F
authors.lastname: Gago
authors.forename: Sonsoles
authors.initials: S
authors.lastname: Velázquez
authors.forename: Antonio
authors.initials: A
authors.lastname: Jiménez-Ruiz
mesh_terms: D000595:Amino Acid Sequence; D018314:Leishmania infantum / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055503:Protein Multimerization
chemical_list: D010455:Peptides; D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase
keywords: Leishmania; dimer quantification assay; enzyme models; protein-protein interactions; trypanothione reductase