A postdoctoral position is available to work in the CNRS in Orléans (France)
in Protein NMR spectroscopy sarting on the 1st of February 2009
In the frame of a multi-partnered French ANR supported consortium on the
structural characterization of the protein RKIP/PEBP active sites, our
laboratory (CBM CNRS UPR4301, Orleans, Fr) offers a one year post doctoral
position (2500 euros gross per month).
The Human Phosphatidylethanolamine Binding Protein (H-PEBP) is a 187 amino
acids protein which is one of the few proteins with a demonstrated metastasis
suppressor activity. Structural information is to be used for the design and
synthesis of small molecules to counter the onset of metastases by potentiating
RKIP/PEBP natural anti-metastasis activity. We propose to use heteronuclear NMR
spectroscopy to identify precisely which amino-acids of H-PEBP are involved in
the binding site of newly synthetised ligands. Since the protein is
successfully expressed in E.coli, doubly labeled 13C, 15N H-PEBP sample have
been successfully produced. 15N HSQC is of very good quality (fig. 1). Backbone
assignment classical triple resonance experiments (800, 950 MHz) have already
been recorded at Frankfurt BMZ (EU_NMR facility). After backbone NH assignment,
ligand binding sites will be determined by the chemical shift perturbation
technique. Ligand conformation in the binding site will be determined by
selective observation of the small unlabelled ligand resonances. These
structural informations will then be fed back to chemists for the rational
synthesis of new ligands with higher affinity for h-PEBP. New ligands will be
assessed by the same NMR techniques.
This position is intended for young researchers with experience in protein
expression and purification together with a strong background in solution
protein NMR spectroscopy as proven by their publication record. Interested
applicants should send a CV and letter to Laurence Jouvensal
(jouvensa@cnrs-orleans.fr) and to Christian Damblon (c.damblon@ulg.ac.be)
