ArticleNature communications2020
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 89 citations in OpenAlex.
- Membrane cholesterol modulates engagement of β-arrestin with the ghrelin receptor.Communications biology · 2026Article
- Beyond Hunger: The Structure, Signaling, and Systemic Roles of Ghrelin.International journal of molecular sciences · 2025Review
- Molecular recognition of two approved drugs Macimorelin and Anamorelin by the growth hormone secretagogue receptor.Acta pharmacologica Sinica · 2025Article
- Ghrelin-LEAP2 interactions along the stomach-liver axis.Endocrine journal · 2025Review
- The structure and function of the ghrelin receptor coding for drug actions.Nature structural & molecular biology · 2025Article
- A Modular Customizable Ligand-Conjugate (LC) System Targeting GhrelinBiomolecules · 2025Article
- How the ghrelin receptor recognizes the acyl-modified orexigenic hormone.Frontiers in molecular neuroscience · 2025Review
- An atomic look at the interface of GHSR and its partners.Computational and structural biotechnology journal · 2024Article
- Transformation of peptides to small molecules in medicinal chemistry: Challenges and opportunities.Acta pharmaceutica Sinica. B · 2024Review
- Article
- G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024Article
- Acyl modifications in bovine, porcine, and equine ghrelins.Frontiers in endocrinology · 2024Article
- Can machine learning 'transform' peptides/peptidomimetics into small molecules? A case study with ghrelin receptor ligands.Molecular diversity · 2023Article
- Improving the Modeling of Extracellular Ligand Binding Pockets in RosettaGPCR for Conformational Selection.International journal of molecular sciences · 2023Article
- Structural basis for motilin and erythromycin recognition by motilin receptor.Science advances · 2023Article
- Ghrelin receptor signaling in health and disease: a biased view.Trends in endocrinology and metabolism: TEM · 2023Review
- Allosteric crosstalk in modular proteins: Function fine-tuning and drug design.Computational and structural biotechnology journal · 2023Review
- Ghrelin infusion into the basolateral amygdala suppresses CTA memory formation in rats via the PI3K/Akt/mTOR and PLC/PKC signaling pathways.Acta pharmacologica Sinica · 2022Article
- Structure of SARS-CoV-2 membrane protein essential for virus assembly.Nature communications · 2022Article
- Binding Domain Characterization of Growth Hormone Secretagogue Receptor.Journal of translational internal medicine · 2022Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ghrelin is a gastric peptide hormone with important physiological functions. The unique feature of ghrelin is its Serine 3 acyl-modification, which is essential for ghrelin's activity. However, it remains to be elucidated why the acyl-modification of ghrelin is necessary for activity. To address these questions, we solved the crystal structure of the ghrelin receptor bound to antagonist. The ligand-binding pocket of the ghrelin receptor is bifurcated by a salt bridge between E124 and R283. A striking feature of the ligand-binding pocket of the ghrelin receptor is a wide gap (crevasse) between the TM6 and TM7 bundles that is rich in hydrophobic amino acids, including a cluster of phenylalanine residues. Mutagenesis analyses suggest that the interaction between the gap structure and the acyl acid moiety of ghrelin may participate in transforming the ghrelin receptor into an active conformation.
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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.