Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: functional and structural investigation.

@article{Heinz1992ChangingTI,
  title={Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: functional and structural investigation.},
  author={Dirk W. Heinz and Sven G Hyberts and Jeffrey W. Peng and John P. Priestle and Gerhard Wagner and Markus G. Gruetter},
  journal={Biochemistry},
  year={1992},
  volume={31 37},
  pages={8755-66}
}
Amino acids in the serine proteinase inhibitor eglin c important for its inhibitory specificity and activity have been investigated by site-directed mutagenesis. The specificity of eglin c could be changed from elastase to trypsin inhibition by the point mutation Leu45----Arg (L45R) in position P1 [nomenclature according to Schechter and Berger (1967) Biochem. Biophys. Res. Commun. 27, 157-162]. Model building studies based on the crystal structure of mutant L45R [Heinz et al. (1991) J. Mol… CONTINUE READING