Ca(II) and Zn(II) Cooperate To Modulate the Structure and Self-Assembly of S100A12.

ABSTRACT: S100A12 is a member of the Ca²⁺ binding S100 family of proteins that functions within the human innate immune system. Zinc sequestration by S100A12 confers antimicrobial activity when the protein is secreted by neutrophils. Here, we demonstrate that Ca²⁺ binding to S100A12's EF-hand motifs and Zn²⁺ binding to its dimeric interface cooperate to induce reversible self-assembly of the protein. Solution and magic angle spinning nuclear magnetic resonance spectroscopy on apo-, Ca²⁺-, Zn²⁺-, and Ca²⁺,Zn²⁺-S100A12 shows that significant metal binding-induced chemical shift perturbations, indicative of conformational changes, occur throughout the polypeptide chain. These perturbations do not originate from changes in the

SUBMITTER: Wang Q 

PROVIDER: S-EPMC7292962 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature