Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site.

@article{Harvey2003MutagenesisOT,
  title={Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site.},
  author={Stephen B. Harvey and Matthew D. Stone and Michael B Martinez and Gary L. Nelsestuen},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 10},
  pages={
          8363-9
        }
}
Site-directed mutagenesis of the 40 N-terminal residues (gamma-carboxyglutamic acid domain) of blood clotting factor VII was carried out to identify sites that improve membrane affinity. Improvements and degree of change included P10Q (2-fold), K32E (13-fold), and insertion of Tyr at position 4 (2-fold). Two other beneficial changes, D33F (2-fold) and A34E (1.5-fold), may exert their impact via influence of K32E. The modification D33E (5.2-fold) also resulted in substantial improvement. The… CONTINUE READING

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