Our research builds upon 30+ years of continuously funded work on the enzymology and structural biology of proteins involved in blood coagulation and on mechanisms of ligand binding.
We are interested in the structural enzymology of proteins responsible for blood coagulation, with the goal of unraveling the molecular architecture and mechanism of the underlying interactions. Our approach uses a combination of conventional (rapid kinetics, protein engineering, X-ray crystallography) and innovative (smFRET, cryo-EM) biophysical techniques.
We currently focus on the interaction of prothrombin with prothrombinase, leading to generation of thrombin and blood clotting, the activation of factor V required for assembly of prothrombinase and the interaction of the thrombin-thrombomodulin complex with protein C that halts the coagulation response. Current studies also focus on factor V short and its interactions with TFPIalpha, protein S and factor Xa. Emerging interests include proteins of the contact pathway like factors IX, XI and XII.
- Structure and dynamics of prothrombin (HL049413)
- Structural enzymology of protein C (HL139554)
- Structural enzymology of factor V activation (HL147821)
Video showing the complex of prothrombin (yellow), fVa (green), and fXa (red).
Read more about the Di Cera Lab’s plenary paper in Blood here: Blood 2022.