Mastoparan binding induces a structural change affecting both the N-terminal and C-terminal domains of calmodulin A 113Cd-NMR study

Abstract113Cd-NMR studies of solutions of cadmium-loaded calmodulin (Cd4CaM) and the tetradecapeptide mastoparan in different ratios show that mastoparan binds to Cd4CaM with high affinity. The off-rate of proteinbound mastoparan is found to be 40 s−1 or less. The binding of one molecule of mastoparan to Cd4CaM is observed to affect all four metal-binding sites, indicating that both the N-terminal and C-terminal globular domains of the protein undergo conformational changes

Rezension zu: Katja Kröss, Die politische Rolle der stadtrömischen Plebs

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The structure of apo-calmodulin:A ¹H NMR examination of the carboxy-terminal domain

AbstractThe structure of the carboxy-terminal domain of bovine calmodulin, TR2C, in the calcium-free form was investigated using two-dimensional 1H NMR. Sequential resonance assignments were made using standard methods. Using information from medium and long range contacts revealed by nuclear Overhauser enhancement, the secondary structure and global fold were determined. The apo protein possesses essentially the same secondary structure as that in the calcium activated form of intact calmodulin. However, the secondary structural elements are rearranged so that the hydrophobic binding pocket is closed in the apo-form