Molecular Dynamics Calculations of Wild Type vs. Mutant Protein C: Relationship Between Binding Affinity to Endothelial Cell Protein C Receptor and Hereditary Disease
Copyright policy )Molecular Dynamics Calculations of Wild Type vs. Mutant Protein C: Relationship Between Binding Affinity to Endothelial Cell Protein C Receptor and Hereditary Disease
Molecular dynamics simulations of the protein C gamma-carboxyglutamic acid (Gla) domain and endothelial cell protein C receptor (EPCR) complex were performed to determine the effect of a hereditary disease, which results in a mutation (Gla 25 --> Lys) in the protein C Gla domain. Our results suggest that the Gla 25 --> Lys mutation causes a significant reduction in the binding force between protein C Gla domain and EPCR due to destabilization of the helix structure of EPCR and displacement of a Ca2+ ion.
- Health Sciences University of Hokkaido Japan
- Nihon University Japan
- Nihon Bunka University Japan
- NEC Soft Japan
Models, Molecular, Models, Genetic, Protein Conformation, Lysine, Genetic Diseases, Inborn, Endothelial Protein C Receptor, Receptors, Cell Surface, Kinetics, Amino Acid Substitution, Antigens, CD, Humans, Computer Simulation, Endothelium, Vascular, 1-Carboxyglutamic Acid, Protein Binding, Protein C
Models, Molecular, Models, Genetic, Protein Conformation, Lysine, Genetic Diseases, Inborn, Endothelial Protein C Receptor, Receptors, Cell Surface, Kinetics, Amino Acid Substitution, Antigens, CD, Humans, Computer Simulation, Endothelium, Vascular, 1-Carboxyglutamic Acid, Protein Binding, Protein C
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