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Table 1 Overview of the 12 examined VKORC1 variants detected in mice and rats

From: Confirmation of warfarin resistance of naturally occurring VKORC1 variants by coexpression with coagulation factor IX and in silico protein modelling

Mutation Species/ref. 2D, 3D prediction 3D modelling
Arg12Trp Mus musculus, Mus spretus[15, 18] 2D: tendency to random coil
3D: clash of side chain
Ser56Pro Rattus norvegicus[14] 2D: tendency to random coil
3D: clash of side chain, less hydrogen bonds
Trp59Arg Rattus spec.[15, 19] 2D: tendency to random coil
3D: change of side chain for ligand
Arg61Leu Mus musculus, Mus spretus[15, 18] 2D: tendency to beta strand
3D: no important differences
Phe63Cys Rattus spec.[15, 19] 2D: tendency to beta strand
3D: clash of side chain
Glu67Lys Rattus spec.[15, 19] 2D, 3D: no important differences
Leu120Gln Rattus norvegicus[14] 2D: conversion of helix to beta strand
3D: missing side chain for ligand binding
Leu128Gln Rattus spec.[14, 15, 19] 2D: partial conversion of helix to beta strand
3D: no differences, interaction with ligand?
Leu128Ser Mus musculus[14, 15] 2D: partial conversion of helix to beta strand
3D: no differences, interaction with ligand?
Tyr139Cys Rattus spec., Mus musculus[14, 15, 19] 2D: tendency to beta strand
3D: no differences, interaction with ligand?
Tyr139Phe Rattus spec.[14, 15, 19] 2D, 3D: no differences, interaction with ligand?
Tyr139Ser Rattus spec.[14, 15, 19] 2D: tendency to random coil
3D: no differences, interaction with ligand?
  1. Results of two- and three-dimensional protein structure predictions are given in the third column. Pictures of 3D modelling based on human VKORC1 protein sequence and the bacterial VKOR structure show the protein parts comprising the respective substitutions. The wild-type protein is displayed in beige, the mutated protein is overlaid in light blue, side chain clashes are highlighted in red.