Abstract
S100 proteins are a sub-family of EF-hand calcium binding proteins that form very similar, unique dimer structures. Although the possibility has been known for many years, no systematic study of the formation of S100 protein heterodimers has been reported. Shaw and coworkers demonstrate the application of a new approach that provides an in-depth evaluation of the distribution of S100 protein homo- and heterodimer and show that the prevalence of heterodimers may be much higher than previously anticipated.
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