Abstract
The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.
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Potts, B., Smith, J., Akke, M. et al. The structure of calcyclin reveals a novel homodimeric fold for S100 Ca2+-binding proteins. Nat Struct Mol Biol 2, 790–796 (1995). https://doi.org/10.1038/nsb0995-790
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DOI: https://doi.org/10.1038/nsb0995-790
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