ArticlePLoS biology2021
Structures of the human cholecystokinin 1 (CCK1) receptor bound to Gs and Gq mimetic proteins provide insight into mechanisms of G protein selectivity.
Article in PLoS biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 86 citations in OpenAlex.
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- Evolutionary conservation and adaptability of cholecystokinin neuropeptide signaling in the sea cucumber Apostichopus japonicus.BMC biology · 2026Article
- Structured water molecules drive activation and G protein selectivity in the GPR174 receptor.PLoS biology · 2026Article
- Photodynamic Activation of Mammalian and Avian Cholecystokinin Type 1 Receptor Outside of the Pancreatic Acinar Cell Microenvironment.International journal of molecular sciences · 2025Article
- Insights into G-protein coupling preference from cryo-EM structures of GNature chemical biology · 2025Article
- Effects of Membrane Cholesterol on the Structure and Function of Selected Class A GPCRs─Challenges and Future Perspectives.Biochemistry · 2025Review
- Cholesterol residence time drives regulation of the G protein-coupled cholecystokinin receptor.Molecular pharmacology · 2025Article
- Molecular basis of ligand binding and receptor activation at the human ANature communications · 2025Article
- Structural insights into the activation of the human prostaglandin EProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bayesian Nonparametric Analysis of Residence Times for Protein-Lipid Interactions in Molecular Dynamics Simulations.Journal of chemical theory and computation · 2025Article
- To activate a G protein-coupled receptor permanently with cell surface photodynamic action in the gastrointestinal tract.World journal of gastroenterology · 2025Review
- Structure and dynamics determine G protein coupling specificity at a class A GPCR.Science advances · 2025Article
- High-resolution cryo-EM using a common LaBScience advances · 2025Article
- Structural insights into the high basal activity and inverse agonism of the orphan receptor GPR6 implicated in Parkinson's disease.Science signaling · 2024Article
- Structure of endothelin ETCommunications biology · 2024Article
- Cholesterol-dependent dynamic changes in the conformation of the type 1 cholecystokinin receptor affect ligand binding and G protein coupling.PLoS biology · 2024Article
- AlphaFold2 structures guide prospective ligand discovery.Science (New York, N.Y.) · 2024Article
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Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
Abstract
G protein-coupled receptors (GPCRs) are critical regulators of cellular function acting via heterotrimeric G proteins as their primary transducers with individual GPCRs capable of pleiotropic coupling to multiple G proteins. Structural features governing G protein selectivity and promiscuity are currently unclear. Here, we used cryo-electron microscopy (cryo-EM) to determine structures of the cholecystokinin (CCK) type 1 receptor (CCK1R) bound to the CCK peptide agonist, CCK-8 and 2 distinct transducer proteins, its primary transducer Gq, and the more weakly coupled Gs. As seen with other Gq/11-GPCR complexes, the Gq-α5 helix (αH5) bound to a relatively narrow pocket in the CCK1R core. Surprisingly, the backbone of the CCK1R and volume of the G protein binding pocket were essentially equivalent when Gs was bound, with the Gs αH5 displaying a conformation that arises from "unwinding" of the far carboxyl-terminal residues, compared to canonically Gs coupled receptors. Thus, integrated changes in the conformations of both the receptor and G protein are likely to play critical roles in the promiscuous coupling of individual GPCRs.
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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 OpenQuestion graph.