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Related Concept Videos

Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

Published on: June 9, 2017

Structural features of the G-protein/GPCR interactions.

Irina S Moreira1

  • 1REQUIMTE/Departamento de Química e Bioquímica, Faculdade de Ciências da Universidade do Porto, Rua do Campo Alegre s/n, 4169-007 Porto, Portugal.

Biochimica Et Biophysica Acta
|September 11, 2013
PubMed
Summary

Structural details of G protein-coupled receptor (GPCR) and G protein interactions remain elusive. This review examines known interfaces, focusing on activation, preassembly, and selective coupling mechanisms in subfamily A GPCRs.

Keywords:
Coupling determinantG protein coupled receptor/G-protein couplingOligomerizationSpecificity

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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay

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Last Updated: May 8, 2026

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
09:12

G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay

Published on: September 10, 2016

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • Extensive research has investigated G protein-GPCR functional interactions using various assays and computational studies.
  • Despite significant efforts, the precise interaction sites and specificities between G proteins and GPCRs are not fully understood.

Purpose of the Study:

  • To review structural details of G protein-GPCR interfaces and recognition sites.
  • To emphasize the impact of activation on GPCR structure.
  • To explore the role of preassembled complexes, selective coupling determinants, and GPCR oligomerization.

Main Methods:

  • Review of existing structural data for G protein-GPCR complexes.
  • Analysis of interface contact sites and molecular architecture.
  • Focus on subfamily A GPCRs and their cognate G proteins.

Main Results:

  • Many contact sites within specific G protein-GPCR complexes have been identified.
  • The 3D molecular architecture of only one receptor-Gα interface is currently known.
  • Fundamental questions about the macromolecular assembly and mechanism persist.

Conclusions:

  • This review synthesizes current structural knowledge of G protein-GPCR interactions for subfamily A.
  • Key aspects discussed include activation-induced structural changes, preassembled complexes, and determinants of selective coupling.
  • Further structural elucidation is needed to answer fundamental questions about these crucial signaling complexes.