Characterization of the interaction between An(III) and a lanthanide binding tag grafted on calmodulin N-ter domain

Key Points

• The main finding reveals distinct characteristics of An(III) binding to calmodulin's N-terminal domain, crucial for understanding metal ion interactions.
• Key evidence indicates a specific binding affinity, which enhances the relevance of lanthanide tagging in biochemical studies.
• Analysis of the molecular interactions employing various biochemical assays shows significant binding characteristics of the lanthanide tag with An(III).
• Supports further exploration of calmodulin's role as a protein scaffold in biotechnological applications involving lanthanide metals.