The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.

@article{Strobl2000TheCS,
  title={The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium.},
  author={Stefan Strobl and Carlos Fern{\'a}ndez-Catal{\'a}n and Marianne Braun and Robert Huber and Hajime Masumoto and Kaku Nakagawa and Akihiro Irie and Hiroyuki Sorimachi and Gleb Bourenkow and Hans D. Bartunik and Kaoru Suzuki and Wolfram Bode},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 2},
  pages={588-92}
}
Calpains (calcium-dependent cytoplasmic cysteine proteinases) are implicated in processes such as cytoskeleton remodeling and signal transduction. The 2.3-A crystal structure of full-length heterodimeric [80-kDa (dI-dIV) + 30-kDa (dV+dVI)] human m-calpain crystallized in the absence of calcium reveals an oval disc-like shape, with the papain-like catalytic domain dII and the two calmodulin-like domains dIV+dVI occupying opposite poles, and the tumor necrosis factor alpha-like beta-sandwich… CONTINUE READING
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