ArticleScientific reports2021
Coevolution underlies GPCR-G protein selectivity and functionality.
Article in Scientific reports, 2021. 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.
- A complex interplay of various intracellular motifs determines G protein binding and activation of muscarinic receptors.Scientific reports · 2026Article
- The GPCR Connection: Linking Alzheimer's Disease and Glioblastoma.Journal of cellular and molecular medicine · 2026Review
- Allostery between Distant Structural Regions Dictates Selectivity in GPCR:G Protein Coupling.Biochemistry · 2026Article
- Article
- Evaluating conserved domains and motifs of decapod gonadotropin-releasing hormone G protein-coupled receptor superfamily.Frontiers in endocrinology · 2024Article
- GPCRome-wide analysis of G-protein-coupling diversity using a computational biology approach.Nature communications · 2023Article
- Evolutionary association of receptor-wide amino acids with G protein-coupling selectivity in aminergic GPCRs.Life science alliance · 2022Article
- Hinge region mediates signal transmission of luteinizing hormone and chorionic gonadotropin receptor.Computational and structural biotechnology journal · 2022Article
- Delineating the conformational landscape and intrinsic properties of the angiotensin II type 2 receptor using a computational study.Computational and structural biotechnology journal · 2022Article
- DEER Analysis of GPCR Conformational Heterogeneity.Biomolecules · 2021Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-coupled receptors (GPCRs) regulate diverse physiological events, which makes them as the major targets for many approved drugs. G proteins are downstream molecules that receive signals from GPCRs and trigger cell responses. The GPCR-G protein selectivity mechanism on how they properly and timely interact is still unclear. Here, we analyzed model GPCRs (i.e. HTR, DAR) and Gα proteins with a coevolutionary tool, statistical coupling analysis. The results suggested that 5-hydroxytryptamine receptors and dopamine receptors have common conserved and coevolved residues. The Gα protein also have conserved and coevolved residues. These coevolved residues were implicated in the molecular functions of the analyzed proteins. We also found specific coevolving pairs related to the selectivity between GPCR and G protein were identified. We propose that these results would contribute to better understandings of not only the functional residues of GPCRs and Gα proteins but also GPCR-G protein selectivity mechanisms.
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