Two clusters of charged residues located in the electropositive face of the von Willebrand factor A1 domain are essential for heparin binding.

@article{RastegarLari2002TwoCO,
  title={Two clusters of charged residues located in the electropositive face of the von Willebrand factor A1 domain are essential for heparin binding.},
  author={Ghassem Rastegar-Lari and Bruno O. Villoutreix and Anne-Sophie Ribba and Paulette Legendre and Dominique Meyer and Dominique Baruch},
  journal={Biochemistry},
  year={2002},
  volume={41 21},
  pages={6668-78}
}
The VWF A1 domain seems to possess two heparin binding regions (residues 565-587 and 633-648) displaying positively charged amino acids, but the overall polyanion-A1 domain interaction scheme remains essentially elusive. To probe this molecular reaction as well as the role of electrostatic forces in VWF-heparin interaction, we performed mutagenesis and molecular modeling experiments. Fifteen mutated rVWFs were expressed [R571A, K572A, R573A, K585A, R571A/K572A/R573A, R578A/R579A, R578A/R579A… CONTINUE READING

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