ArticleScientific reports2016
Structural insights and functional implications of inter-individual variability in β2-adrenergic receptor.
Article in Scientific reports, 2016. 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, 20 citations in OpenAlex.
- Investigating the electrostatics underlying activation of the βBiochimica et biophysica acta. Biomembranes · 2026Article
- Unraveling the Mechanism of Impaired Osteogenic Differentiation in Osteoporosis: Insights fromCells · 2024Article
- Elucidation of a dynamic interplay between a beta-2 adrenergic receptor, its agonist, and stimulatory G protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- MUG: A mutation overview of GPCR subfamily A17 receptors.Computational and structural biotechnology journal · 2023Article
- How Do Molecular Dynamics Data Complement Static Structural Data of GPCRs.International journal of molecular sciences · 2020Review
- Special Issue: Membrane and Receptor Dynamics.The Journal of membrane biology · 2019Article
- Differential Dynamics Underlying the Gln27Glu Population Variant of the βThe Journal of membrane biology · 2019Article
- ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregation.Scientific reports · 2018Article
- Bidirectional Role of β2-Adrenergic Receptor in Autoimmune Diseases.Frontiers in pharmacology · 2018Review
- Identification of a Different Agonist-Binding Site and Activation Mechanism of the Human P2YScientific reports · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human β2-adrenergic receptor (β2AR) belongs to the G protein-coupled receptor (GPCR) family and due to its central role in bronchodilation, is an important drug target. The inter-individual variability in β2AR has been implicated in disease susceptibility and differential drug response. In this work, we identified nine potentially deleterious non-synonymous single nucleotide polymorphisms (nsSNPs) using a consensus approach. The deleterious nsSNPs were found to cluster near the ligand binding site and towards the G-protein binding site. To assess their molecular level effects, we built structural models of these receptors and performed atomistic molecular dynamics simulations. Most notably, in the Phe290Ser variant we observed the rotameric flip of Trp286(6.48), a putative activation switch that has not been reported in β2AR thus far. In contrast, the variant Met82Lys was found to be the most detrimental to epinephrine binding. Additionally, a few of the nsSNPs were seen to cause perturbations to the lipid bilayer, while a few lead to differences at the G-protein coupling site. We are thus able to classify the variants as ranging from activating to damaging, prioritising them for experimental studies.
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