The p53 signaling pathway is a complex multi-component network central to cancer biology. Over 50 percent of all tumors have mutated tumor suppressor p53. The primary focus of my research is structural and biochemical characterization of proteins and protein complexes of p53 pathway, especially, proteins responsible for maintenance of an appropriate level of p53 in the cell.
We use structural biology tools, NMR spectroscopy and X-ray crystallography, in conjunction with other biophysical and biochemical methods to determine 3D structures of proteins and characterize their interactions with specific binding partners. Detailed knowledge of protein structure provides the basis for rational design of new drugs suitable for anti-cancer therapies.