Cited 0 time in webofscience Cited 0 time in scopus

Conformational switch that induces GDP release from Gi

Title
Conformational switch that induces GDP release from Gi
Authors
Ham, DongheeAhn, DonghoonAshim, JanbolatCho, YejinKim, Hee RyungYu, WookyungChung, Ka Young
DGIST Authors
Ham, Donghee; Ahn, Donghoon; Ashim, Janbolat; Cho, Yejin; Kim, Hee Ryung; Yu, Wookyung; Chung, Ka Young
Issue Date
2021-03
Citation
Journal of Structural Biology, 213(1), 107694
Type
Article
Author Keywords
Heterotrimeric guanine nucleotide-binding proteinsGDP releaseStructure
Keywords
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
ISSN
1047-8477
Abstract
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.
URI
http://hdl.handle.net/20.500.11750/13479
DOI
10.1016/j.jsb.2020.107694
Publisher
Academic Press
Related Researcher
  • Author Yu, Wookyung Laboratory of Protein Biophysics
  • Research Interests protein biophysics; protein folding; protein dynamics and conformational change
Files:
There are no files associated with this item.
Collection:
Department of Brain SciencesLaboratory of Protein Biophysics1. Journal Articles


qrcode mendeley

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE