The ever changing moods of calmodulin: how structural plasticity entails transductional adaptability.

@article{Villarroel2014TheEC,
  title={The ever changing moods of calmodulin: how structural plasticity entails transductional adaptability.},
  author={Alvaro Villarroel and Maurizio Taglialatela and Ganeko Bernardo-Seisdedos and Alessandro Alaimo and Jon Agirre and Araitz Alberdi and Carolina Gomis-P{\'e}rez and Maria Virginia Soldovieri and Paolo Ambrosino and Covadonga Malo and Pilar Areso},
  journal={Journal of molecular biology},
  year={2014},
  volume={426 15},
  pages={
          2717-35
        }
}
The exceptional versatility of calmodulin (CaM) three-dimensional arrangement is reflected in the growing number of structural models of CaM/protein complexes currently available in the Protein Data Bank (PDB) database, revealing a great diversity of conformations, domain organization, and structural responses to Ca(2+). Understanding CaM binding is complicated by the diversity of target proteins sequences. Data mining of the structures shows that one face of each of the eight CaM helices can… CONTINUE READING

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