ArticlePLoS computational biology2014
Molecular insights into the dynamics of pharmacogenetically important N-terminal variants of the human β2-adrenergic receptor.
Article in PLoS computational biology, 2014. 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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10 citing papers in PubMed, 30 citations in OpenAlex.
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- Molecular evolution of octopamine receptors inbioRxiv : the preprint server for biology · 2025Article
- Fly casting with ligand sliding and orientational selection supporting complex formation of a GPCR and a middle sized flexible molecule.Scientific reports · 2022Article
- Conformational plasticity and dynamic interactions of the N-terminal domain of the chemokine receptor CXCR1.PLoS computational biology · 2021Article
- The role of ADRB2 gene polymorphisms in malignancies.Molecular biology reports · 2021Review
- How Do Molecular Dynamics Data Complement Static Structural Data of GPCRs.International journal of molecular sciences · 2020Review
- Differential Dynamics Underlying the Gln27Glu Population Variant of the βThe Journal of membrane biology · 2019Article
- Multidisciplinary Consideration of Potential Pathophysiologic Mechanisms of Paradoxical Erythema with Topical Brimonidine Therapy.Advances in therapy · 2016Review
- [Research advances in gene polymorphisms in biological pathways of drugs for asthma].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2016Review
- Structural insights and functional implications of inter-individual variability in β2-adrenergic receptor.Scientific reports · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The human β2-adrenergic receptor (β2AR), a member of the G-protein coupled receptor (GPCR) family, is expressed in bronchial smooth muscle cells. Upon activation by agonists, β2AR causes bronchodilation and relief in asthma patients. The N-terminal polymorphism of β2AR at the 16th position, Arg16Gly, has warranted a lot of attention since it is linked to variations in response to albuterol (agonist) treatment. Although the β2AR is one of the well-studied GPCRs, the N-terminus which harbors this mutation, is absent in all available experimental structures. The goal of this work was to study the molecular level differences between the N-terminal variants using structural modeling and atomistic molecular dynamics simulations. Our simulations reveal that the N-terminal region of the Arg variant shows greater dynamics than the Gly variant, leading to differential placement. Further, the position and dynamics of the N-terminal region, further, affects the ligand binding-site accessibility. Interestingly, long-range effects are also seen at the ligand binding site, which is marginally larger in the Gly as compared to the Arg variant resulting in the preferential docking of albuterol to the Gly variant. This study thus reveals key differences between the variants providing a molecular framework towards understanding the variable drug response in asthma patients.
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