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Article

Mutation of cysteine 214 in Gi1 alpha subunit abolishes its endogenous GTPase activity.

The Biochemical journal - 1 May 2004

Wang Yuren, Tawa Gregory, Smith Deborah, Krishnamurthy Girija, Young Kathleen H

Abstract excerpt

The functional consequences of the mutation of a conserved Cys-214 in Galpha(i1) have been investigated. We reported herein that substitutions of Cys-214 of Galpha(i1) to either alanine or tryptophan abolished the intrinsic GTPase activity. Free phosphate release from [32P]GTP-bound Galpha(i1) C214A or [32P]GTP-bound Galpha(i1) C214W was at least 30-fold lower than that of the wild-type Galpha(i1) in...

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Source

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Identifiers

PMID: 14725508
DOI: 10.1042/BJ20031343
PMCID: PMC1224106

Genes

RGS4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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