Apo-calmodulin binds with its C-terminal domain to the N-methyl-D-aspartate receptor NR1 C0 region.

@article{Akyol2004ApocalmodulinBW,
  title={Apo-calmodulin binds with its C-terminal domain to the N-methyl-D-aspartate receptor NR1 C0 region.},
  author={Zeynep Akyol and Jason A. Bartos and Michelle A Merrill and Laurel A Faga and Olav R Jaren and Madeline A Shea and Johannes W Hell},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 3},
  pages={
          2166-75
        }
}
Calmodulin (CaM) is the major Ca2+ sensor in eukaryotic cells. It consists of four EF-hand Ca2+ binding motifs, two in its N-terminal domain and two in its C-terminal domain. Through a negative feedback loop, CaM inhibits Ca2+ influx through N-methyl-D-aspartate-type glutamate receptors in neurons by binding to the C0 region in the cytosolic tail of the NR1 subunit. Ca2+ -depleted (apo)CaM is pre-associated with a variety of ion channels for fast and effective regulation of channel activities… CONTINUE READING

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