NMR Structures of Thiostrepton Derivatives for Characterization of the Ribosomal Binding Site

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 import...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2011-03, Vol.50 (14), p.3308-3312
Main Authors: Jonker, Hendrik R. A., Baumann, Sascha, Wolf, Antje, Schoof, Sebastian, Hiller, Fabian, Schulte, Kathrin W., Kirschner, Karl N., Schwalbe, Harald, Arndt, Hans-Dieter
Format: Article
Language:English
Subjects:
antibiotics
Binding Sites
drug design
Humans
Molecular Structure
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular
ribosomes
Ribosomes - chemistry
Ribosomes - metabolism
thiopeptides
Thiostrepton - chemistry
Thiostrepton - metabolism
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201003582