Abstract
We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 Å and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.
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Finn, B., Evenäs, J., Drakenberg, T. et al. Calcium-induced structural changes and domain autonomy in calmodulin. Nat Struct Mol Biol 2, 777–783 (1995). https://doi.org/10.1038/nsb0995-777
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DOI: https://doi.org/10.1038/nsb0995-777
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