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NMR structures of thiostrepton derivatives for characterization of the ribosomal binding site

: Jonker, H.R.A.; Baumann, S.; Wolf, A.; Schoof, S.; Hiller, F.; Schulte, K.W.; Kirschner, K.N.; Schwalbe, H.; Arndt, H.-D.


Angewandte Chemie. International edition 50 (2011), Nr.14, S.3308-3312
ISSN: 1433-7851
ISSN: 0044-8249
ISSN: 0570-0833
ISSN: 1521-3773
Fraunhofer SCAI ()

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.