Contributions of the S100A9 C-terminal tail to high-affinity Mn(II) chelation by the host-defense protein human calprotectin.

@article{Brophy2013ContributionsOT,
  title={Contributions of the S100A9 C-terminal tail to high-affinity Mn(II) chelation by the host-defense protein human calprotectin.},
  author={Megan Brunjes Brophy and Toshiki G. Nakashige and Aleth Gaillard and Elizabeth M Nolan},
  journal={Journal of the American Chemical Society},
  year={2013},
  volume={135 47},
  pages={17804-17}
}
Human calprotectin (CP) is an antimicrobial protein that coordinates Mn(II) with high affinity in a Ca(II)-dependent manner at an unusual histidine-rich site (site 2) formed at the S100A8/S100A9 dimer interface. We present a 16-member CP mutant family where mutations in the S100A9 C-terminal tail (residues 96-114) are employed to evaluate the contributions of this region, which houses three histidines and four acidic residues, to Mn(II) coordination at site 2. The results from analytical size… CONTINUE READING
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