ArticleThe journal of physical chemistry. B2015
Structural dynamics and thermostabilization of neurotensin receptor 1.
Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.Communications biology · 2026Review
- Evolutionary scenarios for the specific recognition of nonhomologous endogenous peptides by G protein-coupled receptor paralogs.The Journal of biological chemistry · 2025Article
- Bayesian network models identify cooperative GPCR:G protein interactions that contribute to G protein coupling.The Journal of biological chemistry · 2024Article
- Bayesian network models identify co-operative GPCR:G protein interactions that contribute to G protein coupling.bioRxiv : the preprint server for biology · 2023Article
- Understanding the Stabilization Mechanism of a Thermostable Mutant of Hygromycin B Phosphotransferase by Protein Sector-Guided Dynamic Analysis.ACS omega · 2023Article
- Article
- Yeast-based directed-evolution for high-throughput structural stabilization of G protein-coupled receptors (GPCRs).Scientific reports · 2022Article
- Sequence coevolution and structure stabilization modulate olfactory receptor expression.Biophysical journal · 2022Article
- Allosteric communication regulates ligand-specific GPCR activity.The FEBS journal · 2021Review
- The Dynamics of the Neuropeptide Y Receptor Type 1 Investigated by Solid-State NMR and Molecular Dynamics Simulation.Molecules (Basel, Switzerland) · 2020Article
- Activation Microswitches in Adenosine Receptor ABiochemistry · 2020Article
- Conformational dynamics of a G protein-coupled receptor helix 8 in lipid membranes.Science advances · 2020Article
- Machine Learning for Prioritization of Thermostabilizing Mutations for G-Protein Coupled Receptors.Biophysical journal · 2019Article
- Prediction of Conformation Specific Thermostabilizing Mutations for Class A G Protein-Coupled Receptors.Journal of chemical information and modeling · 2019Article
- Engineering Salt Bridge Networks between Transmembrane Helices Confers Thermostability in G-Protein-Coupled Receptors.Journal of chemical theory and computation · 2018Article
- Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.Scientific reports · 2017Article
- Stabilization of a prokaryotic LAT transporter by random mutagenesis.The Journal of general physiology · 2016Article
- How Can Mutations Thermostabilize G-Protein-Coupled Receptors?Trends in pharmacological sciences · 2016Review
- Rapid Bioinformatic Identification of Thermostabilizing Mutations.Biophysical journal · 2015Article
- Structural prerequisites for G-protein activation by the neurotensin receptor.Nature communications · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The neurotensin receptor NTSR1 binds the peptide agonist neurotensin (NTS) and signals preferentially via the Gq protein. Recently, Grisshammer and co-workers reported the crystal structure of a thermostable mutant NTSR1-GW5 with NTS bound. Understanding how the mutations thermostabilize the structure would allow efficient design of thermostable mutant GPCRs for protein purification, and subsequent biophysical studies. Using microsecond scale molecular dynamics simulations (4 μs) of the thermostable mutant NTSR1-GW5 and wild type NTSR1, we have elucidated the structural and energetic factors that affect the thermostability and dynamics of NTSR1. The thermostable mutant NTSR1-GW5 is found to be less flexible and less dynamic than the wild type NTSR1. The point mutations confer thermostability by improving the interhelical hydrogen bonds, hydrophobic packing, and receptor interactions with the lipid bilayer, especially in the intracellular regions. During MD, NTSR1-GW5 becomes more hydrated compared to wild type NTSR1, with tight hydrogen bonded water clusters within the transmembrane core of the receptor, thus providing evidence that water plays an important role in improving helical packing in the thermostable mutant. Our studies provide valuable insights into the stability and functioning of NTSR1 that will be useful in future design of thermostable mutants of other peptide GPCRs.
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Registered trials
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.