Conclusion
Natural and site-directed mutagenesis experiments are important tools for studying the role of individual amino acids of the VKORCl protein and their involvement in the binding sites for the substrate vitamin K and the antagonist warfarin. Our study supports the hypothesis of different binding sites for vitamin K epoxide and Coumarins and underlines the crucial roles of the coumarin binding motif TYA and the thioredoxin motif CXXC. Understanding the structure and function of the VKORC1 protein is the basis for the development of new anticoagulants with an improved efficacy/side effect profile.
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References
Furie et al. Vitamin K-Dependent Biosynthesis of γ-Carboxyglutamic Acid. Blood 1999; 93: 1798–1808
Rost et al. Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2. Nature 2004; 427(6974): 537–41
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Rost, S., Fregin, A., Hünerberg, M., Müller, C.R., Oldenburg, J. (2006). Site-Directed Mutagenesis of VKORC1, the Target Protein of Coumarin-Type Anticoagulants. In: Scharrer, I., Schramm, W. (eds) 35th Hemophilia Symposium. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-28546-6_51
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