The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor.

@article{Oberst2003TheAO,
  title={The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor.},
  author={Michael D. Oberst and Cicely A Williams and Robert B. Dickson and M. L. Johnson and Chen-Yong Lin},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 29},
  pages={26773-9}
}
The activation of matriptase requires proteolytic cleavage at a canonical activation motif that converts the enzyme from a one-chain zymogen to an active, two-chain protease. In this study, matriptase bearing a mutation in its catalytic triad was unable to undergo this activational cleavage, suggesting that the activating cleavage occurs via a transactivation mechanism where interaction between matriptase zymogen molecules leads to activation of the protease. Using additional point and deletion… CONTINUE READING
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Structural Requirements for Matriptase Activation

  • L. M. Kilpatrick, V. Ellis
  • Biochemical Society Meeting 678,
  • 2002

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