S100 proteins: structure, functions and pathology.

By Christian Heizmann, G. Fritz, B. Schäfer. Frontiers in Bioscience, 2002

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S100A8 and S100A9 in inflammation and cancer. (2006, background): “S100 proteins comprise a family of 23 different members, which are characterized by high homology, low-molecular weight, two calcium-binding EF-hands, and by tissuespecific expression [35–37].”
The endogenous Toll–like receptor 4 agonist S100A8/S100A9 (calprotectin) as innate amplifier of infection, autoimmunity, and cancer (2009, background): “The EF-hand motifs are composed of two -helices flanking a central calcium-binding loop, thus resulting in a classical helix–loop–helix motif [18].”
Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection (2005, background): “Although the physiological function of S100 proteins is not fully understood, members of this protein family are believed to mediate a variety of functions in eukaryotic cell”