NMR characterization of I19L peptide interacting with tubulin

Marie-Jeanne Clement, Isabelle Jourdain, Sylvie Lachkar, Philippe Savarin, Benoit Gigant, Marcel Knossow, Flavio Toma, Andre Sobel & Patrick Curmi
In the present study, we demonstrate that such peptides derived from stathmin family proteins function as potent autonomous inhibitors of tubulin assembly. The NMR structural study of I19L, the most efficient of these peptides, revealed that, while the free peptide has no preferred conformation, it adopts in solution a beta-hairpin structure upon interaction with tubulin, close to that observed in tubulin-SLD crystals by X-ray analysis. Saturation transfer difference NMR (STD-NMR) spectroscopy allowed us to identify...

1 Related Work

Structure analysis of a peptide interacting with tubulin or FtsZ

Philippe Savarin & Patrick Curmi
Understanding the cytoskeleton is required for understanding the dynamic organisation of the intracellular space. In eukaryotic cells, microtubules are one of the major components. It has been demonstrated in the present study that a peptide extracted from the N-terminal of Stathmin-like domain interacts with tubulin and impedes microtubule assembly. Interestingly, it has been demonstrated that one of this peptide was able to interact with FtsZ, the prokaryotic homologue of the tubulin.

Resource Types

  • Text

Publication Year

  • 2010

Data Centers

  • INIST/CNRS - Standard-Based Infrastructure with Distributed Resources