Definition
Calmodulin (CaM) is a small (148 amino acid) ubiquitous protein responsible for decoding oscillatory changes in intracellular calcium and transducing the signal to downstream targets. Four separate calcium (Ca2+)-binding sites are distributed into two globular domains (the N- and C-lobes) tethered together by a linker whose structural flexibility is essential for interactions with its multiple target proteins. So, despite its small size, there are significant complexities in building quantitative mathematical models to accommodate the multitude of different structural (liganded) states that ultimately dictate CaM’s functions. Detailed molecular modeling is beginning to advance our understanding for how this single protein can interact with several unique target proteins in both Ca2+-bound (holoCaM) and Ca2+-free (apoCaM) states.
Detailed Description
CaM is typically described as a dumbbell-shaped protein with two globular domains connected through a central helix (Crivici...
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Waxham, M.N., Cheung, M.S. (2013). Calmodulin, Models of. In: Jaeger, D., Jung, R. (eds) Encyclopedia of Computational Neuroscience. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-7320-6_183-1
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DOI: https://doi.org/10.1007/978-1-4614-7320-6_183-1
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