10.4123/SIDR.000004N.RP
Savarin, Philippe
Philippe
Savarin
Curmi, Patrick
Patrick
Curmi
Structure analysis of a peptide interacting with tubulin or FtsZ
Laboratoire Structure-Activité des Biomolécules Normales et Pathologiques (SABNP), Université d'Evry val d'Essonne, INSERM U829, Batiment Maupertuis, rue du Père Jarlan, 91025 Evry Cedex, France.
2010
Experiment report
Cell differentiation, physiology and dynamics
Structural biology (crystallography, NMR, EM)
Molecular biology and interactions
Bos taurus
Escherichia coli
Synthetic peptide
Multiprotein complexes
Protein-protein interaction detection
NMR Spectroscopy
INIST-CNRS
Zasadzinski, Alain
Alain
Zasadzinski
2010-07-05
2010
en
10.1021/bi0512492
10.1021/bi900556a
10.4123/sidr.000004p.rp
10.4123/sidr.000004q.rp
123 ko
1 page
PDF
Creative Commons License [CC BY-NC-ND 3.0] - http://creativecommons.org/licenses/by-nc-nd/3.0/
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.
Cites: Clément MJ,Jourdain I, Lachkar S, Savarin P, Gigant B, Knossow M, Toma F, Sobel A, Curmi PA. N-Terminal Stathmin-like Peptides Bind Tubulin and Impede Microtubule Assembly. Biochemistry. 2005 Nov;8;44(44):14616-25. PMID: 16262261
Cites: Clément MJ, Kuoch BT, Ha-Duong T, Joshi V, Hamon L, Toma F, Curmi PA, Savarin P. The Stathmin-Derived I19L Peptide Interacts with FtsZ and Alters Its Bundling. Biochemistry. 2009 Oct 20;48(41):9734-44. PMID: 19743836