A fully-funded postdoctoral position is available in the group of Dr. Malene R. Jensen at the Institute for Structural Biology in Grenoble, France. 

The successful candidate will study the structural basis of the assembly of scaffolding complexes in the mitogen-activated protein kinase (MAPK) cell signalling pathways. This involves co-expression of intrinsically disordered scaffold proteins with multiple kinases in insect cells and structural studies of the purified complexes using cryo-EM, X-ray crystallography and NMR spectroscopy. The position is available from the 1st of April 2025, initially for 2 years with a possible extension of up to 4 years.  

More information can be found on the group website: www.jensen-nmr.fr
Facilities
The Institute for Structural Biology is located on the EPN science campus in Grenoble in close proximity to the European Synchrotron Radiation Facility (ESRF), the European Molecular Biology Laboratory (EMBL) Grenoble and the Institute Laue-Langevin (ILL). The IBS has excellent facilities for cryo-EM including access to the Titan Krios installed at the ESRF. In addition, the IBS houses six high-field NMR spectrometers (3 x 600, 700, 850 and 950 MHz) and wetlab facilities for cloning, expression and purification of proteins. Access is facilitated to a number of state-of-the-art research platforms through Integrated Structural Biology Grenoble.

Qualifications
The ideal candidate holds a PhD in chemistry, biochemistry or biophysics (or related discipline) and has experience in co-purification of complexes from insect cells and a proven track-record in structural biology (preferably using cryo-EM or X-ray crystallography). To apply for this position, please send your CV, a motivation letter and the names of two references to malene.jensen@ibs.fr.

Recent relevant publications

T. Orand,  E. Delaforge, A. Lee, J. Kragelj, M. Tengo, L. Tengo, M. Blackledge, E. Boeri Erba, R. J. Davis, A. Palencia, M.R. Jensen 

Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1

T. Orand,  M.R. Jensen 

Binding mechanisms of intrinsically disordered proteins: Insights from experimental studies and structural predictions


L. Mariño Pérez, F.S. Ielasi, A. Lee, E. Delaforge, P. Juyoux, M. Tengo, R.J. Davis, A. Palencia, M.R. Jensen

Structural basis of homodimerization of the JNK scaffold protein JIP2 and its heterodimerization with JIP1


L. Mariño Pérez, F.S. Ielasi, L.M. Bessa, D. Maurin, J. Kragelj, M. Blackledge, N. Salvi, G. Bouvignies, A. Palencia, M.R. Jensen
Nature (2022)
Visualizing protein breathing motions associated with aromatic ring flipping

J. Kragelj, T. Orand, E. Delaforge, L. Tengo, M. Blackledge, A. Palencia, M.R. Jensen
Biomolecules (2021)
Enthalpy-entropy compensation in the promiscuous interaction of an intrinsically disordered protein with homologous protein partners

E. Delaforge, J. Kragelj, L. Tengo, A. Palencia, S. Milles, G. Bouvignies, N. Salvi, M. Blackledge, M.R. Jensen
J. Am. Chem. Soc. (2018)
Deciphering the dynamic interaction profile of an intrinsically disordered protein by NMR exchange spectroscopy

J. Kragelj, A. Palencia, M. Nanao, D. Maurin, G. Bouvignies, M. Blackledge, M.R. Jensen
Proc. Natl. Acad. Sci. (2015)
Structure and dynamics of the MKK7-JNK signalling complex

— 
Dr. Malene R. Jensen | CNRS Research Director | Group Leader SIGNAL
Institut de Biologie Structurale
71, avenue des Martyrs | CS 10090 | 38044 Grenoble CEDEX 9 | France
www.jensen-nmr.fr


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