(PDF) Does the KdpA Subunit From the High Affinity

Does the KdpA Subunit From the High Affinity K+-Translocating P-Type KDP-ATPase Have a Structure Similar to That of K+ Channels?

Biophysical Journal - United States

doi 10.1016/s0006-3495(00)76584-2

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Date

January 1, 2000

Authors

Stewart R. Durell

Evert P. Bakker

H. Robert Guy

Publisher

Elsevier BV

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Amanote Research

Does the KdpA Subunit From the High Affinity K+-Translocating P-Type KDP-ATPase Have a Structure Similar to That of K+ Channels?

Biophysical Journal - United States

doi 10.1016/s0006-3495(00)76584-2

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Does Binding of Ouabain to Human .ALPHA.1-Subunit of Na+,K+-ATPase Affect the ATPase Activity of Adjacent Rat .ALPHA.1-Subunit?

Identification of the Mammalian Na,K-ATPase Β3 Subunit

Primary Structure of a Beta Subunit of Alpha-Dendrotoxin-Sensitive K+ Channels From Bovine Brain.

Improvement in K+-Limited Growth Rate Associated With Expression of the N-Terminal Fragment of One Subunit (KdpA) of the Multisubunit KDP Transporter in Escherichia Coli

Arginine Substitution of a Cysteine in Transmembrane Helix M8 Converts Na+,K+-ATPase to an Electroneutral Pump Similar to H+,k+-ATPase

The zntA Gene of Escherichia Coli Encodes a Zn(II)-Translocating P-Type ATPase

Kinetic Alterations Due to a Missense Mutation in the Na,K-ATPase Α2 Subunit Cause Familial Hemiplegic Migraine Type 2

Substitutions of Glutamate 781 in the Na,K-ATPase Subunit Demonstrate Reduced Cation Selectivity and an Increased Affinity for ATP

CHIF, a Member of the FXYD Protein Family, Is a Regulator of Na,K-ATPase Distinct From the Gamma-Subunit