ArticleProtein science : a publication of the Protein Society2009
Trp fluorescence reveals an activation-dependent cation-pi interaction in the Switch II region of Galphai proteins.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Molecular and functional profiling of Gαi as an intracellular pH sensor.Nature communications · 2025Article
- Kinetics of cone specific G-protein signaling in avian photoreceptor cells.Frontiers in molecular neuroscience · 2023Article
- Article
- A cation-π interaction in a transmembrane helix of vacuolar ATPase retains the proton-transporting arginine in a hydrophobic environment.The Journal of biological chemistry · 2018Article
- Folding of GACS omega · 2018Article
- ImprovedFrontiers in molecular biosciences · 2017Article
- Integration of Fourier Transform Infrared Spectroscopy, Fluorescence Spectroscopy, Steady-state Kinetics and Molecular Dynamics Simulations of Gαi1 Distinguishes between the GTP Hydrolysis and GDP Release Mechanism.The Journal of biological chemistry · 2015Article
- Contribution of each Trp residue toward the intrinsic fluorescence of the Giα1 protein.Protein science : a publication of the Protein Society · 2014Article
- Linking receptor activation to changes in Sw I and II of Gα proteins.Journal of structural biology · 2013Article
- Myristoylation exerts direct and allosteric effects on Gα conformation and dynamics in solution.Biochemistry · 2012Article
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4 authors at 2 institutions in 1 country.
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Abstract
Crystal structures of Galpha(i) (and closely related family member Galpha(t)) reveal much of what we currently know about G protein structure, including changes which occur in Switch regions. Galpha(t) exhibits a low rate of basal (uncatalyzed) nucleotide exchange and an ordered Switch II region in the GDP-bound state, unlike Galpha(i), which exhibits higher basal exchange and a disordered Switch II region in Galpha(i)GDP structures. Using purified Galpha(i) and Galpha(t), we examined the intrinsic tryptophan fluorescence of these proteins, which reports conformational changes associated with activation and deactivation of Galpha proteins. In addition to the expected enhancement in tryptophan fluorescence intensity, activation of GalphaGDP proteins was accompanied by a modest but notable red shift in tryptophan emission maxima. We identified a cation-pi interaction between tryptophan and arginine residues in the Switch II of Galpha(i) family proteins that mediates the observed red shift in emission maxima. Furthermore, amino-terminal myristoylation of Galpha(i) resulted in a less polar environment for tryptophan residues in the GTPase domain, consistent with an interaction between the myristoylated amino terminus and the GTPase domain of Galpha proteins. These results reveal unique insights into conformational changes which occur upon activation and deactivation of G proteins in solution.
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