Arrhythmia mutations in calmodulin can disrupt cooperativity of Ca²⁺ binding and cause misfolding

Key points Mutations in the calmodulin protein (CaM) are associated with arrhythmia syndromes. This study focuses on understanding the structural characteristics of CaM disease mutants and their interactions with the voltage‐gated calcium channel Ca V 1.2. Arrhythmia mutations in CaM can lead to loss of Ca 2+ binding, uncoupling of Ca 2+ binding cooperativity, misfolding of the EF‐hands and altered affinity for the calcium channel. These results...