Calmodulin interactions with IQ peptides from voltage-dependent calcium channels.

@article{Black2005CalmodulinIW,
  title={Calmodulin interactions with IQ peptides from voltage-dependent calcium channels.},
  author={David J. Black and David B. Halling and David V. Mandich and Steen Pedersen and Ruth A. Altschuld and Susan L. Hamilton},
  journal={American journal of physiology. Cell physiology},
  year={2005},
  volume={288 3},
  pages={C669-76}
}
Calmodulin (CaM) functions as a Ca(2+) sensor for inactivation and, in some cases, facilitation of a variety of voltage-dependent Ca(2+) channels. A crucial determinant for CaM binding to these channels is the IQ motif in the COOH-terminal tail of the channel-forming subunit. The binding of CaM to IQ peptides from Lc-, P/Q-, and R-type, but not N-type, voltage-dependent Ca(2+) channels increases the Ca(2+) affinity of both lobes of CaM, producing similar N- and C-lobe Ca(2+) affinities. Ca(2… CONTINUE READING
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