Weikai Li

Weikai Li, Ph.D.

Assistant Professor
Biochemistry and Molecular Biophysics
Research Opportunities
Publications (link to PubMed Central)
  

 
 

 

Office: 251 McDonnell Science Building
Phone: 314-362-8687
Email: liw at biochem.wustl.edu

Research

The Li lab studies the structure and function of two membrane embedded enzymes that support blood coagulation. 1) The vitamin K epoxide reductase (VKOR) couples blood coagulation with oxidative folding of nascent proteins. VKOR is the target of warfarin, the most commonly used oral anticoagulant for treating and preventing thrombosis diseases. 2) The vitamin K dependent γ-carboxylase (VKGC) catalyzes a remarkable reaction that incorporates carbon dioxide into glutamate residues of coagulation factors. This post translational modification is required for the activation of coagulation factors at sites of injury. We use multidisciplinary approaches including X-ray crystallography, biochemistry, membrane biology, and cell biology. The figure shows the first crystal structure of VKOR with its reducing partner (left), and the clustering of wafarin resistance mutations around the active site (right).

Weikai Li research

Most Recent Publications

  • Li, W. and Li, F. Cross-crystal averaging with search models to improve molecular replacement phases. Structure 19:155-161 (2011). [Abstract]

  • Li, W., Schulman, S., Dutton, R., Boyd, D., Beckwith, J. and Rapoport, T.A. Structure of a bacterial homolog of vitamin K epoxide reductase. Nature, 463:507-512 (2010). [Abstract]

  • Schulman, S., Wang, B., Li, W. and Rapoport, T.A. Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners. Proc Natl Acad Sci U S A 107:15027-15032 (2010). [Abstract]

  • Li, W., Schulman, S., Boyd, D., Erlandson, K., Beckwith, J. and Rapoport, T.A. The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal. Mol Cell. 26:511-21 (2007). [Abstract]

  • Li, W., Kamtekar, S., Xiong, Y., Sarkis, G.J., Grindley, N.D. and Steitz, T.A. (2005) Structure of a synaptic gamma-delta resolvase tetramer covalently linked to two cleaved DNAs. Science. 309:1210-1215. [Abstract]