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Article

ATP-binding is stabilized by a stacking interaction within the binding site of Na+/K+ -ATPase.

Biochemical and biophysical research communications - 27 Jun 2003

Hofbauerová Katerina, Kopecký Vladimír, Ettrich Rüdiger, Kubala Martin, Teisinger Jan, Amler Evzen

Abstract excerpt

Site-directed mutagenesis was applied to modify phenylalanines (Phe(475)Trp, Phe(548)Tyr, and both) to generate mutants on the basis of molecular modeling of the ATP-binding domain of Na(+)/K(+)-ATPase, in order to characterize the forces that stabilize ATP in its binding pocket. Each of the muta...

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Share to Adenosine Triphosphate
Share to Chromatography, High Pressure Liquid
Share to Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Structure, Secondary

Share to Protein Structure, Tertiary

Share to Sodium-Potassium-Exchanging ATPase

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Source

Identifiers

PMID: 12804579
DOI: 10.1016/s0006-291x(03)00946-x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-12804579-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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