Structural and molecular changes caused by mutations Thr328Lys and Thr328Arg in FXII associated with hereditary angioedema with normal C1 inhibitor
Methods Three-dimensional structure models of Factor XII (FXII) and active FXII (FXIIa), with
or without mutations, were constructed using MODELLER9v11. Interactions of Factor XIIa
with C1-INH were evaluated using PatchDock v1. 3 for protein-protein docking. Molecular
dynamics simulations were carried out with GROMACS 4.5. 5 software package. Results
Mutations of Thr328 to positively charged and hydrophilic residues Lys or Arg on FXII
molecule cause disruption of a putative O-linked glycosylation site, and altered structural …
or without mutations, were constructed using MODELLER9v11. Interactions of Factor XIIa
with C1-INH were evaluated using PatchDock v1. 3 for protein-protein docking. Molecular
dynamics simulations were carried out with GROMACS 4.5. 5 software package. Results
Mutations of Thr328 to positively charged and hydrophilic residues Lys or Arg on FXII
molecule cause disruption of a putative O-linked glycosylation site, and altered structural …
