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Conformational switch that induces GDP release from Gi

Conformational switch that induces GDP release from Gi
Ham, DongheeAhn, DonghoonAshim, JanbolatCho, YejinKim, Hee RyungYu, WookyungChung, Ka Young
DGIST Authors
Ham, DongheeAhn, DonghoonAshim, JanbolatCho, YejinKim, Hee RyungYu, WookyungChung, Ka Young
Issued Date
Author Keywords
Heterotrimeric guanine nucleotide-binding proteinsGDP releaseStructure
protein structureGalphai1 proteinGalphai2 proteinGalphai3 proteinGalphai4 proteinGalphai5 proteinGbeta6 proteinguanosine diphosphateguanosine triphosphateinhibitory guanine nucleotide binding proteinunclassified drugArticlecarboxy terminal sequenceconformational transitioncontrolled studymolecular dynamicsnonhumanpoint mutationpriority journalprotein bindingprotein expressionprotein functionprotein protein interactionprotein purificationprotein secretion
Heterotrimeric guanine nucleotide-binding proteins (G proteins) are composed of α, β, and γ subunits. Gα switches between guanosine diphosphate (GDP)-bound inactive and guanosine triphosphate (GTP)-bound active states, and Gβγ interacts with the GDP-bound state. The GDP-binding regions are composed of two sites: the phosphate-binding and guanine-binding regions. The turnover of GDP and GTP is induced by guanine nucleotide-exchange factors (GEFs), including G protein-coupled receptors (GPCRs), Ric8A, and GIV/Girdin. However, the key structural factors for stabilizing the GDP-bound state of G proteins and the direct structural event for GDP release remain unclear. In this study, we investigated structural factors affecting GDP release by introducing point mutations in selected, conserved residues in Gαi3. We examined the effects of these mutations on the GDP/GTP turnover rate and the overall conformation of Gαi3 as well as the binding free energy between Gαi3 and GDP. We found that dynamic changes in the phosphate-binding regions are an immediate factor for the release of GDP. © 2021 Elsevier Inc.
Academic Press
Related Researcher
  • 유우경 Yu, Wookyung 뇌과학과
  • Research Interests protein biophysics; protein folding; protein dynamics and conformational change
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Department of Brain Sciences Laboratory of Protein Biophysics 1. Journal Articles


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