ArticleThe Journal of biological chemistry2010
Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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Who cites it
33 citing papers in PubMed, 60 citations in OpenAlex.
- Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.Nature communications · 2026Article
- The intrinsically disordered region of the human parathyroid hormone controls functional amyloid properties.The Journal of biological chemistry · 2026Article
- New Insights into the Structure and Function of Class B1 GPCRs.Endocrine reviews · 2023Article
- Molecular Mechanisms of PTH/PTHrP Class B GPCR Signaling and Pharmacological Implications.Endocrine reviews · 2023Article
- Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics.Scientific reports · 2018Article
- Characterization of a PTH1R missense mutation responsible for Jansen type metaphyseal chondrodysplasia.Odontology · 2017Article
- Gs/Gi Regulation of Bone Cell Differentiation: Review and Insights from Engineered Receptors.Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme · 2016Review
- Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016Review
- Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.Annual review of pharmacology and toxicology · 2016Review
- Structural Basis for Receptor Activity-Modifying Protein-Dependent Selective Peptide Recognition by a G Protein-Coupled Receptor.Molecular cell · 2015Article
- Transmembrane signal transduction by peptide hormones via family B G protein-coupled receptors.Frontiers in pharmacology · 2015Review
- Oligomerization of Family B GPCRs: Exploration in Inter-Family Oligomer Formation.Frontiers in endocrinology · 2015Review
- Glucagon-like peptide-1 receptor ligand interactions: structural cross talk between ligands and the extracellular domain.PloS one · 2014Article
- Insights into the structure of class B GPCRs.Trends in pharmacological sciences · 2014Review
- Selective CGRP and adrenomedullin peptide binding by tethered RAMP-calcitonin receptor-like receptor extracellular domain fusion proteins.Protein science : a publication of the Protein Society · 2013Article
- Noncanonical control of vasopressin receptor type 2 signaling by retromer and arrestin.The Journal of biological chemistry · 2013Article
- Calcium-dependent ligand binding and G-protein signaling of family B GPCR parathyroid hormone 1 receptor purified in nanodiscs.ACS chemical biology · 2013Article
- Bacterial expression and purification of a heterodimeric adrenomedullin receptor extracellular domain complex using DsbC-assisted disulfide shuffling.Protein expression and purification · 2013Article
- A novel approach to quantify G-protein-coupled receptor dimerization equilibrium using bioluminescence resonance energy transfer.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Contributions of fluorescence techniques to understanding G protein-coupled receptor dimerisation.Biophysical reviews · 2012Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The parathyroid hormone receptor (PTH1R) is a class B G protein-coupled receptor that is activated by parathyroid hormone (PTH) and PTH-related protein (PTHrP). Little is known about the oligomeric state of the receptor and its regulation by hormone. The crystal structure of the ligand-free PTH1R extracellular domain (ECD) reveals an unexpected dimer in which the C-terminal segment of both ECD protomers forms an alpha-helix that mimics PTH/PTHrP by occupying the peptide binding groove of the opposing protomer. ECD-mediated oligomerization of intact PTH1R was confirmed in living cells by bioluminescence and fluorescence resonance energy transfer experiments. As predicted by the structure, PTH binding disrupted receptor oligomerization. A receptor rendered monomeric by mutations in the ECD retained wild-type PTH binding and cAMP signaling ability. Our results are consistent with the hypothesis that PTH1R forms constitutive dimers that are dissociated by ligand binding and that monomeric PTH1R is capable of activating G protein.
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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.