Historical Background
Calmodulin (CaM) was first discovered as an unidentified activator of cyclic 3′,5′-nucleotide phosphodiesterase (Cheung 1970). Human CaM is encoded by three distinct genes (CALM1, CALM2, and CALM3), which exhibit minor variations at the nucleotide level, yet express the same amino acid sequence. CaM is a predominantly helical intracellular protein (Fig. 1a) that mediates numerous Ca2+-signaling activities in response to changes in cytosolic Ca2+ levels. CaM can be divided into two globular domains, each containing two cooperatively paired EF-hand motifs, allowing it to bind up to four Ca2+ ions (Kretsinger and Nockolds 1973) (Fig. 1b).
(a) Calcium-free (apo) CaM, and (b) calcium-loaded (holo) CaM. (c) The canonical EF-Hand loop is comprised of a helix-loop-helix structure, with ligands forming a...
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Kirberger, M., Gorkhali, R., Salarian, M., Yang, J.Y. (2018). Calmodulin (CALM1). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101972
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DOI: https://doi.org/10.1007/978-3-319-67199-4_101972
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