NMR structures of thiostrepton derivatives for characterization of the ribosomal binding site
Abstract
Structural probing: The activity of thiostrepton and derivatives with targeted shape changes was determined at their ribosomal binding site by using semisynthesis, NMR structure determination, docking (see picture), and biological evaluation in an integrated fashion. This combination revealed important elements of molecular recognition within the embedded pharmocophore of the target, a composite RNA-protein complex.
