alexa Calcium-induced structural changes and domain autonomy in calmodulin.
Engineering

Engineering

Biosensors Journal

Author(s): Finn BE, Evens J, Drakenberg T, Waltho JP, Thulin E, , Finn BE, Evens J, Drakenberg T, Waltho JP, Thulin E,

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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.
This article was published in Nat Struct Biol and referenced in Biosensors Journal

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