Site-directed mutagenesis of the calcium-binding site of blood coagulation factor XIIIa.

@article{Lai1999SitedirectedMO,
  title={Site-directed mutagenesis of the calcium-binding site of blood coagulation factor XIIIa.},
  author={T S Lai and Thomas F. Slaughter and Keith A. Peoples and Charles S. Greenberg},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 35},
  pages={24953-8}
}
Blood coagulation factor XIIIa is a calcium-dependent enzyme that covalently ligates fibrin molecules during blood coagulation. X-ray crystallography studies identified a major calcium-binding site involving Asp(438), Ala(457), Glu(485), and Glu(490). We mutated two glutamic acid residues (Glu(485) and Glu(490)) and three aspartic acid residues (Asp(472), Asp(476), and Asp(479)) that are in close proximity. Alanine substitution mutants of these residues were constructed, expressed, and purified… CONTINUE READING