Protein-ligand interactions in the lysine-binding site of plasminogen kringle 4 are different in crystal and solution. Electrostatic interactions studied by site-directed mutagenesis exclude Lys35 as an important acceptor in solution.

@article{Nielsen1993ProteinligandII,
  title={Protein-ligand interactions in the lysine-binding site of plasminogen kringle 4 are different in crystal and solution. Electrostatic interactions studied by site-directed mutagenesis exclude Lys35 as an important acceptor in solution.},
  author={Peter R. Nielsen and Katja Einer-Jensen and Thor Las Holtet and Birgit Andersen and Flemming M. Poulsen and Hans Christian Th\ogersen},
  journal={Biochemistry},
  year={1993},
  volume={32 48},
  pages={13019-25}
}
Three amino acid residues previously reported to establish the interactions between lysine-like derivatives and plasminogen kringle 4 have been replaced by other residue types using the methods of site-directed mutagenesis. The effect of these modifications on the binding constant have been measured. The residues are Lys35, Asp57, and Arg71, according to the sequence numbering scheme adapted from the plasminogen kringle 5 domain. The plasminogen kringle 4 derivatives where Lys35 of the native… CONTINUE READING