Abstract
Calmodulin is a major intracellular Ca2+ receptor in eucaryotic cells. The binding of Ca2+ stabilizes one or more conformations of the calmodulin molecule recognized by calmodulin-dependent enzymes such as cyclic nucleotide phosphodiesterase (Cheung, 1967); adenylate cyclase (Cheung et al., 1975; Brostrom et al., 1975); phosphorylase kinase ([Grand et al., 1981; cf review by Malencik & Fischer, 1983); and myosin light chain kinase (cf reviews by Stull, 1980; Small & Sobieszek, 1980; Perry et al., 1984). Large increases in catalytic activity typically result from the association of these enzymes with the calcium-calmodulin complex. A variety of small non-protein ligands also undergo calcium-dependent interactions with calmodulin. The best known of these are the phenothiazine drugs and other pharmacological agents first described by Levin and Weiss (1977). Since evidence suggests that these molecules recognize parts of calmodulin which are the same as (or closely related to) the association sites for calmodulin-dependent enzymes, they have been embraced as models for the characterization of the enzyme-calmodulin interface. However, the information obtainable from them is necessarily incomplete.
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© 1989 Plenum Press, New York
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Anderson, S.R., Malencik, D.A. (1989). Fluorescence Studies of the Calcium-Dependent Functions of Calmodulin. In: Jameson, D.M., Reinhart, G.D. (eds) Fluorescent Biomolecules. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5619-6_14
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DOI: https://doi.org/10.1007/978-1-4684-5619-6_14
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