Design and characterization of calprotectin tetramerization variants for probing the role of oligomerization in receptor activation.

ABSTRACT: Calprotectin is a heterodimer of the S100A8 and S100A9 EF-hand calcium binding proteins, which activates cell surface receptors that signal through the NF-κB inflammatory signaling pathway. Like all S100 proteins, calcium-induced conformational changes in calprotectin are required for binding to partner proteins. In the case of calprotectin, the addition of calcium correlates with the formation of a dimer of heterodimers (heterotetramer). Ligand-induced receptor oligomerization has been proposed as a mechanism of receptor activation. Conversely, it has also been suggested that calprotectin tetramerization can inhibit binding to receptors and serve as an autoinhibitory mechanism. In order to investigate the biological relevance of calprotectin tetramerization and facilitate in-depth biophys

SUBMITTER: Garcia V 

PROVIDER: S-EPMC12720418 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature