Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?

@article{Towler1998FunctionalCO,
  title={Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?},
  author={Eric M. Towler and Sergei V. Gulnik and T. N. Bhat and Dianlin Xie and E Gustschina and T R Sumpter and Nicola Robertson and Christopher Jones and Marlies Sauter and Nikolaus Mueller-Lantzsch and Christine Debouck and Jon. W. Erickson},
  journal={Biochemistry},
  year={1998},
  volume={37 49},
  pages={17137-44}
}
To investigate the biochemical properties of the protease encoded by the human endogenous retrovirus, K10 (HERV-K), 213 amino acids of the 3'-end of the HERV-K protease (PR) open reading frame were expressed in Escherichia coli. Autocatalytic cleavage of the expressed polypeptide resulted in an 18.2 kDa protein which was shown to be proteolytically active against a fluorogenic peptide used as a substrate for HIV-1 protease. On the basis of sequence homology and molecular modeling, the 106 N… CONTINUE READING