Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.

@article{Cabrita2007AeropinFT,
  title={Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap.},
  author={Lisa D. Cabrita and James A Irving and Mary C. Pearce and James C. Whisstock and Stephen P. Bottomley},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 37},
  pages={26802-9}
}
Serpins are metastable proteinase inhibitors. Serpin metastability drives both a large conformational change that is utilized during proteinase inhibition and confers an inherent structural flexibility that renders serpins susceptible to aggregation under certain conditions. These include point mutations (the basis of a number of important human genetic diseases), small changes in pH, and an increase in temperature. Many studies of serpins from mesophilic organisms have highlighted an inverse… CONTINUE READING