Calcium Binding to the Innate Immune Protein Human Calprotectin Revealed by Integrated Mass Spectrometry.

ABSTRACT: Although knowledge of the coordination chemistry and metal-withholding function of the innate immune protein human calprotectin (hCP) has broadened in recent years, understanding of its Ca²⁺-binding properties in solution remains incomplete. In particular, the molecular basis by which Ca²⁺ binding affects structure and enhances the functional properties of this remarkable transition-metal-sequestering protein has remained enigmatic. To achieve a molecular picture of how Ca²⁺ binding triggers hCP oligomerization, increases protease stability, and enhances antimicrobial activity, we implemented a new integrated mass spectrometry (MS)-based approach that can be readily generalized to study other protein-metal and protein-ligand interactions. Three MS-based met

SUBMITTER: Adhikari J 

PROVIDER: S-EPMC7429259 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature