Probing the Dimerization Interface of Leishmania infantum Trypanothione Reductase with Site‐Directed Mutagenesis and Short Peptides. Issue 10 (6th June 2013)

• Record Type: Journal Article
• Authors: Toro, Miguel A.; Sánchez‐Murcia, Pedro A.; Moreno, David; Ruiz‐Santaquiteria, Marta; Alzate, Juan Fernando; Negri, Ana; Camarasa, María‐José; Gago, Federico; Velázquez, Sonsoles; Jiménez‐Ruiz, Antonio
• Is Part Of: Chembiochem. Volume 14:Issue 10(2013)
• Page Start: 1212
• Page End: 1217
• Publication Date: 2013-06-06
• Subjects: dimer quantification assay -- enzyme models -- Leishmania -- protein–protein interactions -- trypanothione reductase; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201200744
• Languages: English
• ISSNs: 1439-4227

Abstract

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.