Comparative analysis of the physical properties of murine and human S100A7: Insight into why zinc piracy is mediated by human but not murine S100A7.

ABSTRACT: S100 proteins are a subfamily of EF-hand calcium-binding proteins found primarily in vertebrate animals. They are distinguished by binding of transition metals and functioning in both the intracellular and extracellular milieu. S100A7 functions in the protection of the skin and mucous membranes and is a biomarker in inflammatory skin disease. A recent study of Neisseria gonorrhoeae infection revealed that human but not murine S100A7 could be used to evade host nutritional immunity. To understand the molecular basis for this difference, we carried out a comparative analysis of the physical and structural properties of human and murine S100A7. The X-ray crystal structure of Ca²⁺-loaded mouse S100A7 (mS100A7) was determined to 1.69 Å resolution, and Ca²⁺-induced conforma

SUBMITTER: Harrison SA 

PROVIDER: S-EPMC10598741 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature