Some of the most important motor proteins in our cells are nanomechanical enzymes that remodel RNA molecules or use RNA binding to initiate cell signaling. RNA helicases, translocases and surveillance proteins all play a vital role in the dynamic life of the cell. We study the molecular basis for their function using a combination of enzymology, crystallography and solution biophysics. Using these approaches, we recently solved the structure of the human antiviral surveillance protein RIG-I, and we have developed a mechanical model for its role in innate immunity. We continue to study the mechanisms of helicase enzymes important in viral replication (such as HCV NS3), and in the remodeling of RNA tertiary structures (such as DEAD-box protein Mss116).
The structure of RIG-I and its ability to bind and differentiate different RNA molecules.