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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(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic...

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Identifiers

PMID: 8596913
DOI: 10.1126/science.271.5254.1413

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

A switch 3 point mutation in the alpha subunit of transducin yields a unique dominant-negative inhibitor.Semantic proximity Read ↗

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Alanine-23 of transducin alpha subunit is involved in defining the affinity for betagammma complex.Semantic proximity Read ↗

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The same mutation in Gsalpha and transducin alpha reveals behavioral differences between these highly homologous G protein alpha-subunits.Semantic proximity Read ↗

Dominant negative mutants of transducin-alpha that block activated receptor.Semantic proximity Read ↗

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Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alpha-subunit.Semantic proximity Read ↗

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Structural Determinants of Constitutive Activation of Gα Proteins: Transducin as a Paradigm.Semantic proximity Read ↗

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Rhodopsin determinants for transducin activation: a gain-of-function approach.Semantic proximity Read ↗

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