Ion-binding properties of recombinant S100beta and two derivatives with either an inactivated Ca2+ site II or a normalized Ca2+ site I.

@article{Durussel1997IonbindingPO,
  title={Ion-binding properties of recombinant S100beta and two derivatives with either an inactivated Ca2+ site II or a normalized Ca2+ site I.},
  author={Isabelle Durussel and Linda J. Van Eldik and Jos A. Cox},
  journal={Biochimica et biophysica acta},
  year={1997},
  volume={1343 2},
  pages={139-43}
}
S100beta contains one unusual and one canonical Ca2+-binding motif. In this study, we measured Ca2+-binding and ensuing conformational changes of recombinant S100beta (rS100beta) and of two mutant forms in which either the canonical loop was inactivated (NoEF) or the unusual one replaced by a canonical one (Caloops). Caloops binds two Ca2+ per monomer with a 3-fold higher affinity than rS100beta; the affinity of NoEF was too low for accurate direct determination. All three proteins bind 3-4 Zn2… CONTINUE READING