publication . Article . 2013

Launching spiking ligands into a protein-protein interface: a promising strategy to destabilize and break interface formation in a tRNA modifying enzyme.

Klaus Reuter; Sarah Cianferani;
  • Published: 14 May 2013 Journal: ACS Chemical Biology, volume 8, pages 1,163-1,178 (issn: 1554-8929, eissn: 1554-8937, Copyright policy)
  • Publisher: American Chemical Society (ACS)
Apart from competitive active-site inhibition of protein function, perturbance of protein–protein interactions by small molecules in oligodomain enzymes opens new perspectives for innovative therapeutics. tRNA–guanine transglycosylase (TGT), a potential target to treat shigellosis, is active only as the homodimer. Consequently, disruption of the dimer interface by small molecules provides a novel inhibition mode. A special feature of this enzyme is the short distance between active site and rim of the dimer interface. This suggests design of expanded active-site inhibitors decorated with rigid, needle-type substituents to spike into potential hot spots of the in...
free text keywords: Molecular Medicine, Biochemistry, General Medicine
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