Article
Changes in steady-state conformational equilibrium resulting from cytoplasmic mutations of the Na,K-ATPase alpha-subunit.
The Journal of biological chemistry - 4 Sept 1998
Boxenbaum N, Daly S E, Javaid Z Z, Lane L K, Blostein R
Abstract excerpt
Mutations comprising either deletion of 32 amino acids from the NH2 terminus (alpha1M32) or a Glu233 --> Lys substitution in the first M2-M3 cytoplasmic loop (E233K) of the alpha1-subunit of the Na, K-ATPase result in a shift in the steady-state E1 left arrow over right arrow E2 conformational eq...
Topics
- Adenosine Triphosphate
- Animals
- Cell Polarity
- Glutamic Acid
- HeLa Cells
- Humans
- Ligands
- Mutation
- Potassium
- Protein Conformation
- Rats
- Recombinant Proteins
- Sequence Deletion
- Sodium
- Sodium-Potassium-Exchanging ATPase
- Vanadates