Evidence for the interaction of valine-10 in cystatin C with the S2 subsite of cathepsin B.

@article{Lindahl1994EvidenceFT,
  title={Evidence for the interaction of valine-10 in cystatin C with the S2 subsite of cathepsin B.},
  author={P. Lindahl and D. Ripoll and M. Abrahamson and J. Mort and A. C. Storer},
  journal={Biochemistry},
  year={1994},
  volume={33 14},
  pages={
          4384-92
        }
}
  • P. Lindahl, D. Ripoll, +2 authors A. C. Storer
  • Published 1994
  • Chemistry, Medicine
  • Biochemistry
  • The interactions between wild-type or mutant recombinant forms of human cystatin C and rat cathepsin B were characterized by measuring progress curves for substrate hydrolysis in the presence of inhibitor. The investigation was guided by the use of computer modeling and explores the possibility that amino acid residues in the N-terminal region of cystatin C interact with substrate-binding regions in the target enzyme. With cystatin C that has Val-10 replaced by an Arg residue (Val10Arg cystatin… CONTINUE READING
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