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Calcium-induced structural changes and domain autonomy in calmodulin.

B E Finn·J Evenäs·T Drakenberg·J P Waltho·E Thulin·S Forsén
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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 A 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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AnimalsCalciumCalmodulinCattleCrystallography, X-RayMagnetic Resonance SpectroscopyProtein ConformationSolutionsStructure-Activity RelationshipComparative StudyJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.

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B E Finn, J Evenäs, T Drakenberg, J P Waltho, E Thulin, S Forsén. 1995. Calcium-induced structural changes and domain autonomy in calmodulin.. https://doi.org/10.1038/nsb0995-777

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