ArticleNature structural & molecular biology2016
Structure and ligand-binding mechanism of the human OX1 and OX2 orexin receptors.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
60 citing papers in PubMed.
- In Silico to In Cerebro-Development of the Orexin Receptor Antagonist "Photorexant" for Photomodulation In Vitro and in Mouse Brains.Angewandte Chemie (International ed. in English) · 2026Article
- Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.Communications biology · 2026Review
- Ultra-large library screening with an evolutionary algorithm in Rosetta (REvoLd).Communications chemistry · 2025Article
- Non-canonical GScientific reports · 2025Article
- Structural insights into GPCR signaling activated by peptide ligands: from molecular mechanism to therapeutic application.Experimental & molecular medicine · 2025Review
- Molecular Insights into the Interaction of Orexin 1 Receptor Antagonists: A Comprehensive Study Using Classical and Quantum Computational Methods.Molecules (Basel, Switzerland) · 2025Article
- RosettaAMRLD: A Reaction-Driven Approach for Structure-Based Drug Design from Combinatorial Libraries with Monte Carlo Metropolis Algorithms.Journal of chemical information and modeling · 2025Article
- Bayesian Nonparametric Analysis of Residence Times for Protein-Lipid Interactions in Molecular Dynamics Simulations.Journal of chemical theory and computation · 2025Article
- In vivo photocontrol of orexin receptors with a nanomolar light-regulated analogue of orexin-B.Cellular and molecular life sciences : CMLS · 2024Article
- G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024Article
- Machine learning models to predict ligand binding affinity for the orexin 1 receptor.Artificial intelligence chemistry · 2024Article
- A novel APP splice variant-dependent marker system to precisely demarcate maturity in SH-SY5Y cell-derived neurons.Scientific reports · 2024Article
- Unraveling the function and structure impact of deleterious missense SNPs in the human OX1R receptor by computational analysis.Scientific reports · 2024Article
- Orexins in apoptosis: a dual regulatory role.Frontiers in cellular neuroscience · 2024Review
- A novel method for identifying key genes in macroevolution based on deep learning with attention mechanism.Scientific reports · 2023Article
- Estradiol-dependent hypocretinergic/orexinergic behaviors throughout the estrous cycle.Psychopharmacology · 2023Review
- Arf GTPase activates the WAVE regulatory complex through a distinct binding site.Science advances · 2022Article
- Fusion protein strategies for cryo-EM study of G protein-coupled receptors.Nature communications · 2022Article
- A study on the effect of JNJ-10397049 on proliferation and differentiation of neural precursor cells.Anatomy & cell biology · 2022Article
- Molecular mechanism of the wake-promoting agent TAK-925.Nature communications · 2022Article
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Authors and funding
13 authors.
Funding
Abstract
The orexin (also known as hypocretin) G protein-coupled receptors (GPCRs) regulate sleep and other behavioral functions in mammals, and are therapeutic targets for sleep and wake disorders. The human receptors hOX1R and hOX2R, which are 64% identical in sequence, have overlapping but distinct physiological functions and potential therapeutic profiles. We determined structures of hOX1R bound to the OX1R-selective antagonist SB-674042 and the dual antagonist suvorexant at 2.8-Å and 2.75-Å resolution, respectively, and used molecular modeling to illuminate mechanisms of antagonist subtype selectivity between hOX1R and hOX2R. The hOX1R structures also reveal a conserved amphipathic α-helix, in the extracellular N-terminal region, that interacts with orexin-A and is essential for high-potency neuropeptide activation at both receptors. The orexin-receptor crystal structures are valuable tools for the design and development of selective orexin-receptor antagonists and agonists.
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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.