Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues

scientific article published on November 1996

Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.271.47.29682
P698PubMed publication ID8939901
P5875ResearchGate publication ID14267095

P2093author name stringLingrel JB
Argüello JM
Kuntzweiler TA
P2860cites workHigh-efficiency transformation of mammalian cells by plasmid DNAQ27860469
Rapid and efficient site-specific mutagenesis without phenotypic selectionQ27860608
Molecular genetics of Na,K-ATPaseQ28237821
A 19-kDa C-terminal tryptic fragment of the alpha chain of Na/K-ATPase is essential for occlusion and transport of cationsQ33634428
Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent.Q34018696
Mutagenesis of the yeast plasma membrane H(+)-ATPase. A novel expression systemQ34089153
Environmental effects on the protonation states of active site residues in bacteriorhodopsinQ34115239
Organization of P-type ATPases: significance of structural diversityQ34289999
Access channel model for the voltage dependence of the forward-running Na+/K+ pumpQ36415691
Occluded cations in active transportQ36587813
Glutamic acid 327 in the sheep alpha 1 isoform of Na+,K(+)-ATPase stabilizes a K(+)-induced conformational changeQ36715565
Glutamate 329 located in the fourth transmembrane segment of the alpha-subunit of the rat kidney Na+,K+-ATPase is not an essential residue for active transport of sodium and potassium ions.Q36755831
Functional reconstitution of the sodium pump. Kinetics of exchange reactions performed by reconstituted Na/K-ATPaseQ37165407
Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPaseQ38344356
Expression in high yield of pig alpha 1 beta 1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae.Q38361905
Voltage dependence of the Na-K pumpQ39644432
Substitutions of glutamate 781 in the Na,K-ATPase alpha subunit demonstrate reduced cation selectivity and an increased affinity for ATP.Q41229967
Kinetic mechanism of inhibition of the Na+-pump and some of its partial reactions by external Na+ (Na+o).Q41338599
Glutamic acid 327 in the sheep alpha 1 isoform of Na+,K(+)-ATPase is a pivotal residue for cation-induced conformational changesQ41918971
Critical effects on catalytic function produced by amino acid substitutions at Asp804 and Asp808 of the alpha1 isoform of Na,K-ATPaseQ42811431
Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitiveQ42816994
Amino Acid Replacement of Asp369 in the Sheep α1 Isoform Eliminates ATP and Phosphate Stimulation of [3]H Ouabain Binding to the Na+,K+-ATPase without Altering the Cation Binding Properties of the EnzymeQ42826068
Comparison of the effects of potassium on ouabain binding to native and site-directed mutants of Na,K-ATPaseQ42829881
Structure-function relationships in the Na,K-ATPase alpha subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzymeQ45790576
Ouabain-receptor interactions in (Na+ + K+)-ATPase preparations. II. Effect of cations and nucleotides on rate constants and dissociation constantsQ48611147
A study on the influence of the concentration of Mg 2+ , P i , K + , Na + , and Tris on (Mg 2+ + P i )-supported g-strophanthin binding to (Na + = K + )activated ATPase from ox brainQ48652031
The effect of membrane potential on the mammalian sodium-potassium pump reconstituted into phospholipid vesicles.Q52428096
Substitutions of serine 775 in the alpha subunit of the Na,K-ATPase selectively disrupt K+ high affinity activation without affecting Na+ interaction.Q54162226
Mutant Glu781-->Ala of the rat kidney Na+,K(+)-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium ions.Q54182264
Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains.Q54223687
Site-directed mutagenesis of a predicted cation binding site of Na, K-ATPase.Q54249506
P433issue47
P407language of work or nameEnglishQ1860
P921main subjecttransmembrane proteinQ424204
P304page(s)29682-29687
P577publication date1996-11-01
P1433published inJournal of Biological ChemistryQ867727
P1476titleAsp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues
P478volume271

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cites work (P2860)
Q74338949Abolishment of proton pumping and accumulation in the E1P conformational state of a plant plasma membrane H+-ATPase by substitution of a conserved aspartyl residue in transmembrane segment 6
Q33723249Analysis of the gastric H,K ATPase for ion pathways and inhibitor binding sites
Q34170836Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli
Q43029611Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus
Q40978877Characterization of disulfide cross-links between fragments of proteolyzed Na,K-ATPase. Implications for spatial organization of trans-membrane helices
Q43559851Chimeras of X+, K+-ATPases. The M1-M6 region of Na+, K+-ATPase is required for Na+-activated ATPase activity, whereas the M7-M10 region of H+, K+-ATPase is involved in K+ de-occlusion
Q34474628Conformational coupling: the moving parts of an ion pump.
Q44355334Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation
Q42645434Constitutive activation of gastric H+,K+-ATPase by a single mutation
Q59060684Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state
Q22337247Crystal structure of the sodium–potassium pump
Q48820652Electrophysiological Analysis of the Mutated Na,K-ATPase Cation Binding Pocket
Q73735513Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket
Q36888091Extensive random mutagenesis analysis of the Na+/K+-ATPase alpha subunit identifies known and previously unidentified amino acid residues that alter ouabain sensitivity--implications for ouabain binding
Q44504061Functional consequences of alterations to Ile279, Ile283, Glu284, His285, Phe286, and His288 in the NH2-terminal part of transmembrane helix M3 of the Na+,K(+)-ATPase
Q73571682Functional role of cysteine residues in the (Na,K)-ATPase alpha subunit
Q77754922Glu-857 moderates K+-dependent stimulation and SCH 28080-dependent inhibition of the gastric H,K-ATPase
Q33704448Hypothermia-induced dystonia and abnormal cerebellar activity in a mouse model with a single disease-mutation in the sodium-potassium pump.
Q44703982Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases.
Q45115007Identification of the transmembrane metal binding site in Cu+-transporting PIB-type ATPases
Q44083667Importance of Glu(282) in transmembrane segment M3 of the Na(+),K(+)-ATPase for control of cation interaction and conformational changes
Q33699327Jeanne Mannery Fisher Memorial Lecture 1998. Structure-function studies of the sodium pump
Q27930906Manganese selectivity of pmr1, the yeast secretory pathway ion pump, is defined by residue gln783 in transmembrane segment 6. Residue Asp778 is essential for cation transport
Q44550963Mechanism of proton transport by plant plasma membrane proton ATPases
Q48376290Molecular cloning of Na(+)-ATPase cDNA from a marine alga, Heterosigma akashiwo
Q77796450Mutagenesis of glutamate 820 of the gastric H+,K+-ATPase alpha-subunit to aspartate decreases the apparent ATP affinity
Q48571523Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, associated with familial rapid-onset dystonia parkinsonism, interfere with Na+ interaction by distinct mechanisms.
Q24300347Osteocyte control of bone formation via sclerostin, a novel BMP antagonist
Q46136802Point mutations in the extracytosolic loop between transmembrane segments M5 and M6 of the yeast Pma1 H+-ATPase: alanine-scanning mutagenesis
Q37416960Quaternary benzyltriethylammonium ion binding to the Na,K-ATPase: a tool to investigate extracellular K+ binding reactions
Q36495106Role of transmembrane segment M8 in the biogenesis and function of yeast plasma-membrane H(+)-ATPase
Q37023818Roles of transmembrane segment M1 of Na+,K+-ATPase and Ca2-ATPase, the gatekeeper and the pivot.
Q48946231Significance of the glutamic acid residues Glu334, Glu959, and Glu960 of the alpha subunits of Torpedo Na+, K+ pumps for transport activity and ouabain binding
Q46024279Sites of reaction of the gastric H,K-ATPase with extracytoplasmic thiol reagents.
Q28141760Sperm motility is dependent on a unique isoform of the Na,K-ATPase
Q35569174Structural insights into the binding of cardiac glycosides to the digitalis receptor revealed by solid-state NMR
Q34810867Structure-function relationships in membrane segment 6 of the yeast plasma membrane Pma1 H(+)-ATPase
Q47729683Structure-function relationships of E1-E2 transitions and cation binding in Na,K-pump protein
Q34180462Structure-function relationships of Na(+), K(+), ATP, or Mg(2+) binding and energy transduction in Na,K-ATPase.
Q28286446The CorA Mg2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore
Q42691139The cadmium transport sites of CadA, the Cd2+-ATPase from Listeria monocytogenes
Q40837253The current produced by the E779A mutant rat Na(+)/K(+) pump alpha1-subunit expressed in HEK 293 cells
Q41829313The negative charge of glutamic acid-820 in the gastric H+,K+-ATPase alpha-subunit is essential for K+ activation of the enzyme activity
Q46130612The role of loop 6/7 in folding and functional performance of Na,K-ATPase
Q37262471The selectivity of the Na(+)/K(+)-pump is controlled by binding site protonation and self-correcting occlusion
Q34655307The sodium pump. Its molecular properties and mechanics of ion transport
Q46375266Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na+ transport, and Gln-923 (M8) is essential for Na,K-ATPase activity

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