ArticleNature communications2024
Structural basis of ligand recognition and activation of the histamine receptor family.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Hypersensitivity reactions to contrast media: Part 2. Prevention of recurrent hypersensitivity reactions in adults. Updated guidelines by the ESUR Contrast Media Safety Committee.European radiology · 2025Guideline
- Antidiabetic Properties of Histamine H1 Receptor Antagonists: A Systematic Review.Antioxidants (Basel, Switzerland) · 2026Review
- Sensomics-based characterization of cinnamon-like aroma inFood chemistry: X · 2026Article
- Binding affinities for histamine receptors 1 to 4: Systematic comparison of ligands from the Psychoactive Drug Screening Program KMolecular pharmacology · 2026Review
- Persistent prostaglandin E2 upregulation and hormonal multi-resistance: A hypothesis for long COVID.Biochemistry and biophysics reports · 2026Article
- Neuro-Immune Crosstalk: Molecular Mechanisms, Biological Functions, Diseases, and Therapeutic Targets.MedComm · 2026Review
- Activity-restoring mutations in the histamine HProtein science : a publication of the Protein Society · 2026Article
- Identification of histidine decarboxylase and its multi-enzyme cascade system for cost-efficient biosynthesis of carcinine.3 Biotech · 2025Article
- A Radiolabeled Photoswitchable G Protein-Coupled Receptor Antagonist Enlightens Ligand Binding Kinetics Associated with Photoswitching.Journal of the American Chemical Society · 2025Article
- Structural insights into ligand recognition and G protein preferences across histamine receptors.Communications biology · 2025Article
- Cryo-EM Structures and AlphaFold3 Models of Histamine Receptors Reveal Diverse Ligand Binding and G Protein Bias.Pharmaceuticals (Basel, Switzerland) · 2025Article
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
Histamine is a biogenic amine that is critical in various physiological and pathophysiological processes, including but not limited to allergic reactions, wakefulness, gastric acid secretion and neurotransmission. Here, we determine 9 cryo-electron microscopy (cryo-EM) structures of the 4 histamine receptors in complex with four different G protein subtypes, with endogenous or synthetic agonists bound. Inside the ligand pocket, we identify key motifs for the recognition of histamine, the distinct binding orientations of histamine and three subpockets that facilitate the design of specific ligands. In addition, we also identify key residues responsible for the selectivity of immethridine. Moreover, we reveal distinct structural features as determinants of Gq vs. Gs or Gs vs. Gi coupling differences among the histamine receptors. Our study provides a structural framework for understanding the ligand recognition and G protein coupling of all 4 histamine receptors, which may facilitate the rational design of ligands targeting these receptors.
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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 Socratic graph.