ArticleScientific reports2019
Ligand-Induced Conformational Dynamics of A Tyramine Receptor from Sitophilus oryzae.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Thermo-responsive Bioink for Personalized 3D Printed Scaffolds with Antioxidant and Fibroblast Delivery to Accelerate Diabetic Wound Healing.Biomaterials research · 2025Article
- Progress in the research of immunotherapy‑related hyperprogression (Review).Molecular and clinical oncology · 2024Review
- Specificity of Monoterpene Interactions with Insect Octopamine and Tyramine Receptors: Insights fromACS omega · 2023Article
- Octopamine and tyramine signalling in Aedes aegypti: Molecular characterization and insight into potential physiological roles.PloS one · 2023Article
- Study of tyramine-binding mechanism and insecticidal activity of oil extracted from Eucalyptus againstFrontiers in chemistry · 2022Article
- pH-Dependent Conformations of an Antimicrobial Spider Venom Peptide, Cupiennin 1a, from Unbiased HREMD Simulations.ACS omega · 2021Article
- G-Protein Coupled Receptors (GPCRs): Signaling Pathways, Characterization, and Functions in Insect Physiology and Toxicology.International journal of molecular sciences · 2021Review
- Review
- LILRB4, from the immune system to the disease target.American journal of translational research · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tyramine receptor (TyrR) is a biogenic amine G protein-coupled receptor (GPCR) associated with many important physiological functions in insect locomotion, reproduction, and pheromone response. Binding of specific ligands to the TyrR triggers conformational changes, relays the signal to G proteins, and initiates an appropriate cellular response. Here, we monitor the binding effect of agonist compounds, tyramine and amitraz, to a Sitophilus oryzae tyramine receptor (SoTyrR) homology model and their elicited conformational changes. All-atom molecular dynamics (MD) simulations of SoTyrR-ligand complexes have shown varying dynamic behavior, especially at the intracellular loop 3 (IL3) region. Moreover, in contrast to SoTyrR-tyramine, SoTyrR-amitraz and non-liganded SoTyrR shows greater flexibility at IL3 residues and were found to be coupled to the most dominant motion in the receptor. Our results suggest that the conformational changes induced by amitraz are different from the natural ligand tyramine, albeit being both agonists of SoTyrR. This is the first attempt to understand the biophysical implication of amitraz and tyramine binding to the intracellular domains of TyrR. Our data may provide insights into the early effects of ligand binding to the activation process of SoTyrR.
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