What is it about?
The strutcural analysis of the binding of calcium-free calmodulin to a peptide of a putative binding domain of the cardiac calcium channel (CaV1.2 ) using NMR. This compares and contrasts to the calcium loaded structure recently published elsewhere.
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Why is it important?
Calmodulin mediates the cardiac calcium channel inactivation. This paper shows calmodulin still binds to the channel, but with a reduced affinity and different binding pattern.
Perspectives
This was my first paper, from work in my PhD., after being beaten to the complete atomic structure of the calcium loaded calmodulin by other groups
Daniel Myatt
Read the Original
This page is a summary of: Apo calmodulin binding to the L-type voltage-gated calcium channel Cav1.2 IQ peptide, Biochemical and Biophysical Research Communications, February 2007, Elsevier,
DOI: 10.1016/j.bbrc.2006.12.070.
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