Cation binding and conformational changes in VILIP and NCS-1, two neuron-specific calcium-binding proteins.

@article{Cox1994CationBA,
  title={Cation binding and conformational changes in VILIP and NCS-1, two neuron-specific calcium-binding proteins.},
  author={Jos A. Cox and Isabelle Durussel and Michelle Comte and Serge Nef and Patrick C Nef and Stefan E. Lenz and Eckart D. Gundelfinger},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 52},
  pages={32807-13}
}
VILIP and NCS-1, neural-specific, 22-kDa Ca(2+)-binding proteins possessing four EF-hands, were expressed in Escherichia coli to study their divalent cation properties. Flow dialysis (Ca2+ binding) and equilibrium gel filtration (Mg2+ binding) revealed that both recombinant proteins possess only two active metal-binding sites, which can accommodate either Ca2+ or Mg2+. VILIP binds cations without cooperativity with intrinsic affinity constants K'Ca of 1.0 x 10(6) M-1 and K'Mg of 4.8 x 10(3) M-1… CONTINUE READING