Residues of the Fourth Transmembrane Segments of the Na,K-ATPase and the Gastric H,K-ATPase Contribute to Cation Selectivity

We have generated protein chimeras to investigate the role of the fourth transmembrane segments (TM4) of the Na,K- and gastric H,K-ATPases in determining the distinct cation selectivities of these two pumps. Based on a helical wheel analysis, three residues of TM4 of the Na,K-ATPase were changed to...

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Veröffentlicht in:	The Journal of biological chemistry 2000-01, Vol.275 (3), p.1749-1756
Hauptverfasser:	Mense, Martin, Dunbar, Lisa A., Blostein, Rhoda, Caplan, Michael J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Amino Acid Sequence Animals Cations - metabolism Electrophysiology H(+)-K(+)-Exchanging ATPase - chemistry Hydrogen-Ion Concentration Inhibitory Concentration 50 Kinetics Molecular Sequence Data Mutation Ouabain - pharmacology Potassium - metabolism Recombinant Fusion Proteins - chemistry Sequence Homology, Amino Acid Sodium - metabolism Sodium-Potassium-Exchanging ATPase - chemistry Stomach - enzymology Vanadates - pharmacology Xenopus Xenopus laevis - metabolism
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