Backbone resonance assignments for G protein αi3 subunit in the GTP-bound state

Yoko Mase, Mariko Yokogawa, Masanori Osawa, Ichio Shimada

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Guanine-nucleotide binding proteins (G proteins) act as molecular switches in signaling pathways, by coupling the activation of G protein-coupled receptors (GPCRs) at the cell surface to intracellular responses. In the resting state, G protein forms a heterotrimer, consisting of GDP-bound form of the G protein α subunit (Gα(GDP)) and G protein βγ subunit (Gβγ). Ligand binding to GPCRs promotes the GDP-GTP exchange on Gα, leading to the dissociation of the GTP-bound form of Gα (Gα(GTP)) and Gβγ. Then, Gα(GTP) and Gβγ bind to their downstream effector enzymes or ion channels and regulate their activities, leading to a variety of cellular responses. Finally, Gα hydrolyzes the bound GTP to GDP and returns to the resting state by re-associating with Gβγ. G proteins are classified with four major families based on the amino acid sequences of Gα: i/o, s, q/11, and 12/13. Each family transduces the signaling from different GPCRs to the specific effectors. Here, we established the backbone resonance assignments of human Gαi3, a member of the i/o family, with a molecular weight of 41 K in complex with a GTP analogue, GTPγS.

Original languageEnglish
Pages (from-to)217-220
Number of pages4
JournalBiomolecular NMR Assignments
Issue number2
Publication statusPublished - 2012 Oct
Externally publishedYes


  • G protein α subunit
  • GPCR-signaling
  • Heterotrimeric guanine-nucleotide binding protein
  • Signal transduction

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry


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