Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in α‐subunit of renal Na,K‐ATPase

Mutations to Asp804 and Asp808 in the α‐subunit almost abolish Na,K‐ATPase activity, but high‐affinity binding of [3H]ATP or [3H]ouabain at equilibrium and E1–E2 transitions are preserved. Titration of K+‐ion displacement of [3H]ATP or [3H]ouabain shows that the mutations interfere with occlusion of...

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Veröffentlicht in:	FEBS letters 1997-01, Vol.400 (2), p.206-210
Hauptverfasser:	Pedersen, Per Amstrup, Rasmussen, Jakob H, Nielsen, Jesper M, Jorgensen, Peter L
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Aspartic Acid Mutagenesis Mutagenesis, Site-Directed Na,K-ATPase Ouabain Ouabain - metabolism Potassium Potassium - metabolism Sodium Sodium - metabolism Sodium-Potassium-Exchanging ATPase - genetics Sodium-Potassium-Exchanging ATPase - metabolism Yeast expression Yeasts
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