Intrinsic disorder mediates cooperative signal transduction in STIM1.

@article{Furukawa2014IntrinsicDM,
  title={Intrinsic disorder mediates cooperative signal transduction in STIM1.},
  author={Yukio Furukawa and Shunsuke Teraguchi and Takahisa Ikegami and Onur Dagliyan and Lin Jin and Damien Hall and Nikolay V. Dokholyan and Keiichi Namba and Shizuo Akira and Tomohiro Kurosaki and Yoshihiro Baba and Daron M. Standley},
  journal={Journal of molecular biology},
  year={2014},
  volume={426 10},
  pages={
          2082-97
        }
}
Intrinsically disordered domains have been reported to play important roles in signal transduction networks by introducing cooperativity into protein-protein interactions. Unlike intrinsically disordered domains that become ordered upon binding, the EF-SAM domain in the stromal interaction molecule (STIM) 1 is distinct in that it is ordered in the monomeric state and partially unfolded in its oligomeric state, with the population of the two states depending on the local Ca(2+) concentration… CONTINUE READING

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