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Article

Conversion of the low affinity ouabain-binding site of non-gastric H,K-ATPase into a high affinity binding site by substitution of only five amino acids.

The Journal of biological chemistry - 12 May 2006

Qiu Li Yan, Swarts Herman G P, Tonk Elisa C M, Willems Peter H G M, Koenderink Jan B, De Pont Jan Joep H H M

Abstract excerpt

P-type ATPases of the IIC subfamily exhibit large differences in sensitivity toward ouabain. This allows a strategy in which ouabain-insensitive members of this subfamily are used as template for mutational elucidation of the ouabain-binding site. With this strategy, we recently identified seven amino acids in Na,K-ATPase that conferred high affinity ouabain binding to gastric H,K-ATPase (Qiu, L. Y., Krieger, E.,...

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Identifiers

PMID: 16531406
DOI: 10.1074/jbc.M600551200

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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.

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