Mutational analysis of the transin (rat stromelysin) autoinhibitor region demonstrates a role for residues surrounding the "cysteine switch".

@article{Park1991MutationalAO,
  title={Mutational analysis of the transin (rat stromelysin) autoinhibitor region demonstrates a role for residues surrounding the "cysteine switch".},
  author={Ae Ja Park and Lynn M Matrisian and Amy F. Kells and Roger Pearson and Zhen Ya Yuan and Marc Navre},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 3},
  pages={1584-90}
}
The family of mammalian extracellular matrix metalloproteases (MMPs) are secreted by cells in an inactive (latent) proenzyme form. A highly conserved amino acid sequence, PRCGVPDV, is found near the COOH-terminal end of the pro-domain of these MMPs and believed to act as an "autoinhibitor." Recent studies (Springman, E. B., Angleton, E. L., Birkedal-Hansen, H., and Wart, H. E. V. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 364-368) indicate the Cys of this sequence ligands to the active-site… CONTINUE READING
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