Cation binding and conformational changes in VILIP and NCS-1, two neuron-specific calcium-binding proteins
JA Cox, I Durussel, M Comte, S Nef, P Nef… - Journal of Biological …, 1994 - ASBMB
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× 10 (6) M-1 and K'Mg of 4.8× 10 (3) M-1. Mg2+ antagonizes Ca2+ binding by …
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× 10 (6) M-1 and K'Mg of 4.8× 10 (3) M-1. Mg2+ antagonizes Ca2+ binding by …