Interactions between the conserved arginine from the target peptide and the calmodulin linker region. Arg812 from the MLCK peptide hydrogen bonds with the two residues of calmodulin at the beginning and end of the flexible tether between the N-terminal and C-terminal domains. This arginine, found one residue before the C-terminal hydrophobic anchor of the peptide, is well conserved in calmodulin peptides. Calmodulin is light grey and the MLCK peptide is dark grey. The structure was rendered in Insight using PDB coordinates 1CDL.
This figure appeared as figure 13 in the book chapter:
Nelson, M.R., Chazin W.J., "Calmodulin as a calcium sensor" in
Calmodulin and Signal Transduction (1998) L.J. Van Eldik and
D.M. Watterson, eds. Academic Press, San Diego, pp. 17-64.
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