ArticlePloS one2015
Integrating solid-state NMR and computational modeling to investigate the structure and dynamics of membrane-associated ghrelin.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Computational structure prediction of lanthipeptides with NMR data reveals underappreciated peptide flexibility.Protein science : a publication of the Protein Society · 2025Article
- Molecular mechanism of agonism and inverse agonism in ghrelin receptor.Nature communications · 2022Article
- Acylation, a Conductor of Ghrelin Function in Brain Health and Disease.Frontiers in physiology · 2022Review
- The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2021Review
- Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020Review
- Integration of Cell-Free Expression and Solid-State NMR to Investigate the Dynamic Properties of Different Sites of the Growth Hormone Secretagogue Receptor.Frontiers in pharmacology · 2020Article
- A Benchmark for Homomeric Enzyme Active Site Structure Prediction Highlights the Importance of Accurate Modeling of Protein Symmetry.ACS omega · 2019Article
- Side Chain Orientation of Tryptophan Analogues Determines Agonism and Inverse Agonism in Short Ghrelin Peptides.ChemMedChem · 2019Article
- Structure and dynamics of G protein-coupled receptor-bound ghrelin reveal the critical role of the octanoyl chain.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural Model of Ghrelin Bound to its G Protein-Coupled Receptor.Structure (London, England : 1993) · 2019Article
- The Rosetta All-Atom Energy Function for Macromolecular Modeling and Design.Journal of chemical theory and computation · 2017Article
- Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The peptide hormone ghrelin activates the growth hormone secretagogue receptor 1a, also known as the ghrelin receptor. This 28-residue peptide is acylated at Ser3 and is the only peptide hormone in the human body that is lipid-modified by an octanoyl group. Little is known about the structure and dynamics of membrane-associated ghrelin. We carried out solid-state NMR studies of ghrelin in lipid vesicles, followed by computational modeling of the peptide using Rosetta. Isotropic chemical shift data of isotopically labeled ghrelin provide information about the peptide's secondary structure. Spin diffusion experiments indicate that ghrelin binds to membranes via its lipidated Ser3. Further, Phe4, as well as electrostatics involving the peptide's positively charged residues and lipid polar headgroups, contribute to the binding energy. Other than the lipid anchor, ghrelin is highly flexible and mobile at the membrane surface. This observation is supported by our predicted model ensemble, which is in good agreement with experimentally determined chemical shifts. In the final ensemble of models, residues 8-17 form an α-helix, while residues 21-23 and 26-27 often adopt a polyproline II helical conformation. These helices appear to assist the peptide in forming an amphipathic conformation so that it can bind to the membrane.
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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.