ArticleThe journal of physical chemistry. B2013
Thermostabilization of the β1-adrenergic receptor correlates with increased entropy of the inactive state.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Conformational dynamics and multimodal interaction of Paxillin with the focal adhesion targeting domain.Science advances · 2025Article
- Conformational dynamics and multi-modal interaction of Paxillin with the Focal Adhesion Targeting Domain.bioRxiv : the preprint server for biology · 2025Article
- Understanding the Stabilization Mechanism of a Thermostable Mutant of Hygromycin B Phosphotransferase by Protein Sector-Guided Dynamic Analysis.ACS omega · 2023Article
- Activation mechanism of the human Smoothened receptor.Biophysical journal · 2023Article
- Machine Learning for Prioritization of Thermostabilizing Mutations for G-Protein Coupled Receptors.Biophysical journal · 2019Article
- Dynamic Role of the G Protein in Stabilizing the Active State of the Adenosine AStructure (London, England : 1993) · 2019Article
- Engineering Salt Bridge Networks between Transmembrane Helices Confers Thermostability in G-Protein-Coupled Receptors.Journal of chemical theory and computation · 2018Article
- How Can Mutations Thermostabilize G-Protein-Coupled Receptors?Trends in pharmacological sciences · 2016Review
- Structural dynamics and energetics underlying allosteric inactivation of the cannabinoid receptor CB1.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural dynamics and thermostabilization of neurotensin receptor 1.The journal of physical chemistry. B · 2015Article
- Conformational preferences underlying reduced activity of a thermophilic ribonuclease H.Journal of molecular biology · 2015Article
- Rapid Computational Prediction of Thermostabilizing Mutations for G Protein-Coupled Receptors.Journal of chemical theory and computation · 2014Article
- Dynamic behavior of the active and inactive states of the adenosine A(2A) receptor.The journal of physical chemistry. B · 2014Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The dynamic nature of GPCRs is a major hurdle in their purification and crystallization. Thermostabilization can facilitate GPCR structure determination, as has been shown by the structure of the thermostabilized β1-adrenergic receptor (β1AR) mutant, m23-β1AR, which has been thermostabilized in the inactive state. However, it is unclear from the structure how the six thermostabilizing mutations in m23-β1AR affect receptor dynamics. We have used molecular dynamics simulations in explicit solvent to compare the conformational ensembles for both wild type β1AR (wt-β1AR) and m23-β1AR. Thermostabilization results in an increase in the number of accessible microscopic conformational states within the inactive state ensemble, effectively increasing the side chain entropy of the inactive state at room temperature, while suppressing large-scale main chain conformational changes that lead to activation. We identified several diverse mechanisms of thermostabilization upon mutation. These include decrease of long-range correlated movement between residues in the G-protein coupling site to the extracellular region (Y227A(5.58), F338M(7.48)), formation of new hydrogen bonds (R68S), and reduction of local stress (Y227(5.58), F327(7.37), and F338(7.48)). This study provides insights into microscopic mechanisms underlying thermostability that leads to an understanding of the effect of these mutations on the structure of the receptor.
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