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

The evolving model of calmodulin structure,function and activation

AbstractRecent high-resolution crystal and solution structures have answered many long-standing questions about calmodulin and its various conformational states. However, there is still much to learn