ArticlePloS one2014
Glucagon-like peptide-1 receptor ligand interactions: structural cross talk between ligands and the extracellular domain.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- A New Function of the S100-A4 Protein (Mts1): Mts1 Stimulates the Activation of Cytotoxic Lymphocytes via the TREM-1 Receptor.International journal of molecular sciences · 2026Article
- Multivalent γ-PGA-Exendin-4 Conjugates to Target Pancreatic β-Cells.Chembiochem : a European journal of chemical biology · 2022Article
- A quinoxaline-based compound ameliorates bone loss in ovariectomized mice.Experimental biology and medicine (Maywood, N.J.) · 2021Article
- A role of PLC/PKC-dependent pathway in GLP-1-stimulated insulin secretion.Journal of molecular medicine (Berlin, Germany) · 2017Review
- Landmark studies on the glucagon subfamily of GPCRs: from small molecule modulators to a crystal structure.Acta pharmacologica Sinica · 2015Review
- HX-MS2 for high performance conformational analysis of complex protein states.Protein science : a publication of the Protein Society · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Activation of the glucagon-like peptide-1 receptor (GLP-1R) in pancreatic β-cells potentiates insulin production and is a current therapeutic target for the treatment of type 2 diabetes mellitus (T2DM). Like other class B G protein-coupled receptors (GPCRs), the GLP-1R contains an N-terminal extracellular ligand binding domain. N-terminal truncations on the peptide agonist generate antagonists capable of binding to the extracellular domain, but not capable of activating full length receptor. The main objective of this study was to use Hydrogen/deuterium exchange (HDX) to identify how the amide hydrogen bonding network of peptide ligands and the extracellular domain of GLP-1R (nGLP-1R) were altered by binding interactions and to then use this platform to validate direct binding events for putative GLP-1R small molecule ligands. The HDX studies presented here for two glucagon-like peptide-1 receptor (GLP-1R) peptide ligands indicates that the antagonist exendin-4[9-39] is significantly destabilized in the presence of nonionic detergents as compared to the agonist exendin-4. Furthermore, HDX can detect stabilization of exendin-4 and exendin-4[9-39] hydrogen bonding networks at the N-terminal helix [Val19 to Lys27] upon binding to the N-terminal extracellular domain of GLP-1R (nGLP-1R). In addition we show hydrogen bonding network stabilization on nGLP-1R in response to ligand binding, and validate direct binding events with the extracellular domain of the receptor for putative GLP-1R small molecule ligands.
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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.