ArticleProceedings of the National Academy of Sciences of the United States of America2012
Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Ligand-dependent G protein dynamics underlying opioid efficacy.Nature structural & molecular biology · 2026Article
- Activation dynamics of a water-soluble human mu-opioid receptor.The Journal of biological chemistry · 2026Article
- NovelGenes & diseases · 2026Article
- Review
- Ligand-dependent G protein dynamics underlying opioid signaling efficacy.bioRxiv : the preprint server for biology · 2025Article
- Comparative structural insights and functional analysis for the distinct unbound states of Human AGO proteins.Scientific reports · 2025Article
- Influence of expression and purification protocols on Gα biochemical activity: kinetics of plant and mammalian G protein cycles.Frontiers in molecular biosciences · 2025Article
- A neurodevelopmental disorder mutation locks G proteins in the transitory pre-activated state.Nature communications · 2024Article
- Article
- Structural and Functional Implication of Natural Variants of Gαs.International journal of molecular sciences · 2023Article
- GCR1 Positively Regulates UV-B- and Ethylene-Induced Stomatal Closure via Activating GPA1-Dependent ROS and NO Production.International journal of molecular sciences · 2022Article
- Towards resolution of a paradox in plant G-protein signaling.Plant physiology · 2022Article
- The Conformational Dynamics of Heterotrimeric G Proteins During GPCR-Mediated Activation.Sub-cellular biochemistry · 2022Review
- Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.International journal of molecular sciences · 2021Review
- Research Advances in Heterotrimeric G-Protein α Subunits and Uncanonical G-Protein Coupled Receptors in Plants.International journal of molecular sciences · 2021Review
- A universal allosteric mechanism for G protein activation.Molecular cell · 2021Article
- An atypical heterotrimeric Gα protein has substantially reduced nucleotide binding but retains nucleotide-independent interactions with its cognate RGS protein and Gβγ dimer.Journal of biomolecular structure & dynamics · 2020Article
- Receptor-Like Kinase Phosphorylation of Arabidopsis Heterotrimeric G-Protein Gα -Subunit AtGPA1.Proteomics · 2019Article
- Rational design of a heterotrimeric G protein α subunit with artificial inhibitor sensitivity.The Journal of biological chemistry · 2019Article
- GCR1 and GPA1 coupling regulates nitrate, cell wall, immunity and light responses in Arabidopsis.Scientific reports · 2019Article
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Authors and funding
4 authors.
Funding
Abstract
Proteins with similar crystal structures can have dissimilar rates of substrate binding and catalysis. Here we used molecular dynamics simulations and biochemical analysis to determine the role of intradomain and interdomain motions in conferring distinct activation rates to two Gα proteins, Gα(i1) and GPA1. Despite high structural similarity, GPA1 can activate itself without a receptor, whereas Gα(i1) cannot. We found that motions in these proteins vary greatly in type and frequency. Whereas motion is greatest in the Ras domain of Gα(i1), it is greatest in helices αA and αB from the helical domain of GPA1. Using protein chimeras, we show that helix αA from GPA1 is sufficient to confer rapid activation to Gα(i1). Gα(i1) has less intradomain motion than GPA1 and instead displays interdomain displacement resembling that observed in a receptor-heterotrimer crystal complex. Thus, structurally similar proteins can have distinct atomic motions that confer distinct activation mechanisms.
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