Ca
2+-free calmodulin (apocalmodulin) binds target proteins and alters their function. Apocalmodulin has roles in the cell that apparently do not require the ability to bind Ca
2+ at all, and these roles appear to be essential for cell's metabolism. Small-angle X-ray scattering (SAXS) results indicate that the overall conformation of apocalmodulin remains unchanged, but the conformation for the C-domain changes from the closed to semi-open conformation upon binding the target proteins. The conformational change would be induced by electrostatic interactions and subsequent van der Waals interactions and it can cause changes in the Ca
2+ affinity of the apocalmodulin-target protein complex. An analysis of residue pairs between calmodulin and target peptides suggests that apocalmodulin recognizes Ca
2+-dependent calmodulin binding proteins, utilizing a new motif different from IQ motif.
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