Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site.

European journal of biochemistry - 1 Oct 2004

Krumscheid Rita, Ettrich Rüdiger, Sovová Zofie, Susánková Klára, Lánský Zdenek, Hofbauerová Katerina, Linnertz Holger, Teisinger Jan, Amler Evzen, Schoner Wilhelm

Abstract excerpt

The structural stability of the large cytoplasmic domain (H(4)-H(5) loop) of mouse alpha(1) subunit of Na(+)/K(+) ATPase (L354-I777), the number and the location of its binding sites for 2'-3'-O-(trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and p-nitrophenylphosphate (pNPP) were investigated. C- and N-terminal shortening revealed that neither part of the phosphorylation (P)-domain are necessary for TNP-ATP...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphate
Share to Cytoplasm

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Fluorescent Dyes

Share to Glutathione Transferase

Share to Kidney

Share to Protein Tyrosine Phosphatases

Share to Sodium-Potassium-Exchanging ATPase

Source

Identifiers

PMID: 15373838
DOI: 10.1111/j.1432-1033.2004.04330.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site.PMID 15373838Read ↗

Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, associated with familial rapid-onset dystonia parkinsonism, interfere with Na+ interaction by distinct mechanisms.Semantic proximity Read ↗

The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.Semantic proximity Read ↗

The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations.Semantic proximity Read ↗

Thr-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.Semantic proximity Read ↗

Conformational dynamics of the Na+/K+-ATPase probed by voltage clamp fluorometry.Semantic proximity Read ↗

Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase.Semantic proximity Read ↗

Interaction of nucleotides with Asp(351) and the conserved phosphorylation loop of sarcoplasmic reticulum Ca(2+)-ATPase.Semantic proximity Read ↗

Crystal structure of Na+, K(+)-ATPase in the Na(+)-bound state.Semantic proximity Read ↗

Mutation of aspartate 804 of Na(+),K(+)-ATPase modifies the cation binding pocket and thereby generates a high Na(+)-ATPase activity.Semantic proximity Read ↗

Role of conserved TGDGVND-loop in Mg2+ binding, phosphorylation, and energy transfer in Na,K-ATPase.Semantic proximity Read ↗

Structure-function relationships based on ATP binding and cation occlusion at equilibrium in Na,K-ATPase.Semantic proximity Read ↗

The amino acid sequence 442GDASE446 in Na/K-ATPase is an important motif in forming the high and low affinity ATP binding pockets.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.