Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution.

@article{Otterbein2002CrystalSO,
  title={Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution.},
  author={Ludovic R Otterbein and Jolanta Kordowska and Carlos Witte-Hoffmann and C. -L. Albert Wang and Roberto Dom{\'i}nguez},
  journal={Structure},
  year={2002},
  volume={10 4},
  pages={557-67}
}
S100A6 is a member of the S100 family of Ca(2+) binding proteins, which have come to play an important role in the diagnosis of cancer due to their overexpression in various tumor cells. We have determined the crystal structures of human S100A6 in the Ca(2+)-free and Ca(2+)-bound states to resolutions of 1.15 A and 1.44 A, respectively. Ca(2+) binding is responsible for a dramatic change in the global shape and charge distribution of the S100A6 dimer, leading to the exposure of two… CONTINUE READING

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