Article
A calbindin D9k mutant with reduced calcium affinity and enhanced cooperativity. Metal ion binding, stability, and structural studies.
Biochemistry - 18 Oct 1994
Linse S, Bylsma N R, Drakenberg T, Sellers P, Forsén S, Thulin E, Svensson L A, Zajtzeva I, Zajtsev V, Marek J
Abstract excerpt
In the native calcium-binding protein calbindin D9k (M(r) 8.700; 75aa; 2 EF-hands), the backbone carbonyl oxygen of Glu60 coordinates the Ca2+ ion in the C-terminal site (site II). The carboxylate group of the same residue forms a hydrogen bond to a water molecule that constitutes a Ca2+ ligand i...
Topics
- Aspartic Acid
- Binding Sites
- Cadmium
- Calbindins
- Calcium
- Calorimetry, Differential Scanning
- Crystallography, X-Ray
- Drug Stability
- Glutamic Acid
- Hot Temperature
- Hydrogen Bonding
- Magnetic Resonance Spectroscopy
- Molecular Structure
- Mutation
- S100 Calcium Binding Protein G