Consequences of Mutations to the Phosphorylation Site of the α-Subunit of Na,K-ATPase for ATP Binding and E1−E2 Conformational Equilibrium

Expression of Na,K-ATPase in yeast allowed targeting of αβ-units with lethal substitutions at the phosphorylation site α1(D369N)β1 and α1(D369A)β1 at the cell surface at the same concentration of α-subunit and [3H]ouabain binding sites as for wild type Na,K-ATPase. Phosphorylation and reaction with...

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Veröffentlicht in:	Biochemistry (Easton) 1996-12, Vol.35 (50), p.16085-16093
Hauptverfasser:	Pedersen, Per Amstrup, Rasmussen, Jakob H, Jørgensen, Peter L
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Sequence Animals Binding Sites Cloning, Molecular Conserved Sequence Kinetics Macromolecular Substances Models, Chemical Mutagenesis, Site-Directed Ouabain - metabolism Phosphorylation Point Mutation Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Saccharomyces cerevisiae Sodium-Potassium-Exchanging ATPase - chemistry Sodium-Potassium-Exchanging ATPase - metabolism Swine Thermodynamics
Online-Zugang:	Volltext
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