Inhibitory mechanism of a cross-class serpin, the squamous cell carcinoma antigen 1.

@article{Masumoto2003InhibitoryMO,
  title={Inhibitory mechanism of a cross-class serpin, the squamous cell carcinoma antigen 1.},
  author={Kiyonari Masumoto and Yasuhisa Sakata and Kazuhiko Arima and Isao Nakao and Kenji Izuhara},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 46},
  pages={45296-304}
}
The squamous cell carcinoma antigen (SCCA) 1 and its homologous molecule, SCCA2, belong to the ovalbumin-serpin family. Although SCCA2 inhibits serine proteinases such as cathepsin G and mast cell chymase, SCCA1 targets cysteine proteinases such as cathepsin S, K, L, and papain. SCCA1 is therefore called a cross-class serpin. The inhibitory mechanism of the standard serpins is well characterized; those use a suicide substrate-like inhibitory mechanism during which an acyl-enzyme intermediate by… CONTINUE READING

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