ArticleBiophysical journal2013
Domain-opening and dynamic coupling in the α-subunit of heterotrimeric G proteins.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
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- Conserved Residues in the Gα interface show subtype specificity in Gβγ coupling.bioRxiv : the preprint server for biology · 2026Article
- Impact of Intracellular Proteins on μ-Opioid Receptor Structure and Ligand Binding.The journal of physical chemistry. B · 2025Article
- The conformational space of RNase P RNA in solution.Nature · 2025Article
- Complementary Pocket and Network-Based Approach to Search for Spike Protein Allosteric Pocket Sites.ACS omega · 2023Article
- Protocol for structure determination of SARS-CoV-2 main protease at near-physiological-temperature by serial femtosecond crystallography.STAR protocols · 2022Article
- Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing.Structure (London, England : 1993) · 2021Article
- Seeking the exclusive binding region of phenylalkylamine derivatives on human T-type calcium channels via homology modeling and molecular dynamics simulation approach.Pharmacology research & perspectives · 2021Article
- Activating Mutations of the G-protein Subunit α 11 Interdomain Interface Cause Autosomal Dominant Hypocalcemia Type 2.The Journal of clinical endocrinology and metabolism · 2020Article
- Structural and dynamical description of the enzymatic reaction of a phosphohexomutase.Structural dynamics (Melville, N.Y.) · 2019Article
- Comparative structural dynamic analysis of GTPases.PLoS computational biology · 2018Article
- Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web.Journal of visualized experiments : JoVE · 2017Article
- Recent Progress in Understanding the Conformational Mechanism of Heterotrimeric G Protein Activation.Biomolecules & therapeutics · 2017Review
- Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics.PLoS computational biology · 2016Review
- Dynamic Coupling and Allosteric Networks in the α Subunit of Heterotrimeric G Proteins.The Journal of biological chemistry · 2016Article
- Identification of a Novel Homozygous Nonsense Mutation Confirms the Implication of GNAT1 in Rod-Cone Dystrophy.PloS one · 2016Article
- Integrating protein structural dynamics and evolutionary analysis with Bio3D.BMC bioinformatics · 2014Article
- Kinesin-5 allosteric inhibitors uncouple the dynamics of nucleotide, microtubule, and neck-linker binding sites.Biophysical journal · 2014Article
- Mapping the structural and dynamical features of kinesin motor domains.PLoS computational biology · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterotrimeric G proteins are conformational switches that turn on intracellular signaling cascades in response to the activation of G-protein-coupled receptors. Receptor activation by extracellular stimuli promotes a cycle of GTP binding and hydrolysis on the G protein α-subunit (Gα). Important conformational transitions occurring during this cycle have been characterized from extensive crystallographic studies of Gα. However, the link between the observed conformations and the mechanisms involved in G-protein activation and effector interaction remain unclear. Here we describe a comprehensive principal component analysis of available Gα crystallographic structures supplemented with extensive unbiased conventional and accelerated molecular dynamics simulations that together characterize the response of Gα to GTP binding and hydrolysis. Our studies reveal details of activating conformational changes as well as the intrinsic flexibility of the α-helical domain that includes a large-scale 60° domain opening under nucleotide-free conditions. This result is consistent with the recently reported open crystal structure of Gs, the stimulatory G protein for adenylyl cyclase, in complex with the α2 adrenergic receptor. Sets of unique interactions potentially important for the conformational transition are also identified. Moreover simulations reveal nucleotide-dependent dynamical couplings of distal regions and residues potentially important for the allosteric link between functional sites.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.