X-ray crystallographic characterisation of selective PPARγ ligands and deciphering the structure-function relationship of the tRNA import

Structural characterisation of macromolecules is important for understanding their function. Novel ligands targeting PPARα/γ were characterized by in vitro TR-FRET binding assay and the promising ligands were used in crystallization experiments to elucidate the mode of binding and use the structural information gathered to improve the designed molecules. The structural analysis of the Arabidopsis thaliana Tric1 protein revealed an oligomeric assembly of SAM domains. A mutational approach was implemented to disrupt the oligomerization of Tric1 SAM domain to elucidate the potential role on protein function and plant physiology. The results suggest an important role for oligomerization in mitochondrial RNA import.