Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds.

@article{Tan1996BlockingTC,
  title={Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds.},
  author={R Y Tan and Yoko Mabuchi and Zenon Grabarek},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 13},
  pages={7479-83}
}
Calcium-dependent regulation of intracellular processes is mediated by proteins that on binding Ca2+ assume a new conformation, which enables them to bind to their specific target proteins and to modulate their function. Calmodulin (CaM) and troponin C, the two best characterized Ca2+-regulatory proteins, are members of the family of Ca2+-binding proteins utilizing the helix-loop-helix structural motif (EF-hand). Herzberg, Moult, and James (Herzberg, O., Moult, J., and James, M.N.G. (1986) J… CONTINUE READING

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