Uncoupling of GTP binding from target stimulation by a single mutation in the transducin alpha subunit.

doi:10.1126/science.271.5254.1413

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Article

Uncoupling of GTP binding from target stimulation by a single mutation in the transducin alpha subunit.

Science (New York, N.Y.) - 8 Mar 1996

Mittal R, Erickson J W, Cerione R A

Abstract excerpt

Glutamic acid-203 of the alpha subunit of transducin (alphaT) resides within a domain that undergoes a guanosine triphosphate (GTP)-induced conformational change that is essential for effector recognition. Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha...

Topics

3',5'-Cyclic-GMP Phosphodiesterases
Adenosine Diphosphate Ribose
Alanine
Animals
Base Sequence
Cattle
Enzyme Activation
Glutamic Acid
Guanosine 5'-O-(3-Thiotriphosphate)
Guanosine Diphosphate
Guanosine Triphosphate
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Conformation

Protein Structure, Secondary

Protein Structure, Tertiary

Recombinant Fusion Proteins

Rhodopsin

Source

Open in PubMed

Identifiers

PMID: 8596913
DOI: 10.1126/science.271.5254.1413

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8596913-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Uncoupling of GTP binding from target stimulation by a single mutation in the transducin alpha subunit.PMID 8596913Read ↗

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