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. Author manuscript; available in PMC: 2015 Mar 18.
Published in final edited form as: Nat Commun. 2014 Sep 18;5:4896. doi: 10.1038/ncomms5896

Figure 5. CaM conformations when bound to NaV channels compared to CaV channels and CaMKII.

Figure 5

(A-E) Unique arrangement of CaM relative to the IQ domains in the NaV1.5/-Ca2+ structure (A), the NaV1.2/Ca2+ structure (B); a CaV1.2 structure (C, PDB ID: 2BE6); a CaV2.1 structure (D, PDB ID: 3DVM) and autoinhibitory (CaM binding) peptide in CaMKII (E, PDB ID: 1CDM). CaM N-lobe and C-lobe are colored yellow and green, respectively and the orientation of IQ motifs or autoinhibitory peptide is indicated with a color gradient (N-terminus blue and C-terminus red). The positions of IQ(M) amino acid residues on the IQ domains or the 302AI303 amino acid residues in the CaMKII autoinhibitory peptide are demarcated with two black lines. The cartoon figures are shown below each structure to illustrate the difference of the CaM-Nav1.2 interactions. CaM wraps around the NaV IQ domains in the left-handed fashion in contrast to the right-handed wrapping seen in CaV structures and in CaMKII.