ArticleNature chemical biology2023
Ligand recognition and allosteric modulation of the human MRGPRX1 receptor.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 40 citations in OpenAlex.
- De novo design of miniproteins targeting GPCRs.Nature · 2026Article
- International Union of Basic and Clinical Pharmacology. CXXII. Applying an objective evaluation to the status of class A orphan G protein-coupled receptors.Pharmacological reviews · 2026Review
- Structural basis for positive allosteric regulation of CB2 receptor.Nature communications · 2026Article
- Structural insight into ligand binding and activation of the orphan GPCR Mas1.The EMBO journal · 2026Article
- Endosomal MrGPRX1 signaling sensitizes TRPV1 to enhance itch.Frontiers in molecular neuroscience · 2026Article
- Theoretical-Experimental Analysis to Elucidate the Mechanism of Action of Novel Anabolic Agents.Molecules (Basel, Switzerland) · 2025Article
- Terpene-Based Thiazole Hydrazines as Negative Allosteric Modulators of MRGPRX4: In Vitro Evaluation and Binding Site Analysis.ACS medicinal chemistry letters · 2025Article
- Self-supervised learning for generalizable particle picking in cryo-EM micrographs.Cell reports methods · 2025Article
- Article
- Antimicrobial Peptide Signaling in Skin Diseases.JID innovations : skin science from molecules to population health · 2025Review
- Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery.Nature reviews. Drug discovery · 2025Review
- Molecular Glues: A New Approach to Modulating GPCR Signaling Bias.Biochemistry · 2025Review
- High-affinity agonists reveal recognition motifs for the MRGPRD GPCR.Cell reports · 2024Article
- Article
- AlphaFold2 structures guide prospective ligand discovery.Science (New York, N.Y.) · 2024Article
- Pathology of pain and its implications for therapeutic interventions.Signal transduction and targeted therapy · 2024Review
- MRGPRX4 mediates phospho-drug-associated pruritus in a humanized mouse model.Science translational medicine · 2024Article
- G protein-coupled receptors (GPCRs): advances in structures, mechanisms, and drug discovery.Signal transduction and targeted therapy · 2024Review
- Accurate cryo-EM protein particle picking by integrating the foundational AI image segmentation model and specialized U-Net.bioRxiv : the preprint server for biology · 2024Article
- The MRGPR family of receptors in immunity.Immunity · 2024Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
The human MAS-related G protein-coupled receptor X1 (MRGPRX1) is preferentially expressed in the small-diameter primary sensory neurons and involved in the mediation of nociception and pruritus. Central activation of MRGPRX1 by the endogenous opioid peptide fragment BAM8-22 and its positive allosteric modulator ML382 has been shown to effectively inhibit persistent pain, making MRGPRX1 a promising target for non-opioid pain treatment. However, the activation mechanism of MRGPRX1 is still largely unknown. Here we report three high-resolution cryogenic electron microscopy structures of MRGPRX1-Gαq in complex with BAM8-22 alone, with BAM8-22 and ML382 simultaneously as well as with a synthetic agonist compound-16. These structures reveal the agonist binding mode for MRGPRX1 and illuminate the structural requirements for positive allosteric modulation. Collectively, our findings provide a molecular understanding of the activation and allosteric modulation of the MRGPRX1 receptor, which could facilitate the structure-based design of non-opioid pain-relieving drugs.
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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.