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Article

Specific structural requirements for the inhibitory effect of thapsigargin on the Ca2+ ATPase SERCA.

The Journal of biological chemistry - 23 Apr 2004

Xu Cheng, Ma Hailun, Inesi Giuseppe, Al-Shawi Marwan K, Toyoshima Chikashi

Abstract excerpt

Mutational analysis of amino acid residues lining the thapsigargin (TG) binding cavity at the interface of the membrane surface and cytosolic headpiece was performed in the Ca(2+) ATPase (SERCA-1). Specific mutations such as F256V, I765A, and Y837A reduce not only the apparent affinity of the ATPase for TG but also the maximal inhibitory effect. The effect of mutations is dependent on the type and size of the...

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Identifiers

PMID: 14970206
DOI: 10.1074/jbc.M313263200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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