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Related Concept Videos

G Protein-coupled Receptors01:15

G Protein-coupled Receptors

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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...
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Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

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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,...
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G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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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.
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GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

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Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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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...
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GPCR Desensitization01:12

GPCR Desensitization

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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Related Experiment Video

Updated: Oct 3, 2025

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
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Function-related dynamics of GPCRs.

Takumi Ueda1, Shunsuke Imai2, Ichio Shimada3

  • 1Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|February 15, 2022
PubMed
Summary
This summary is machine-generated.

Nuclear Magnetic Resonance (NMR) reveals that G protein-coupled receptors (GPCRs) dynamically shift between multiple conformations. These findings clarify function-related conformational dynamics crucial for GPCR signaling.

Keywords:
Adenosine receptorAdrenergic receptorGPCRMembrane proteinsNMR

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Pharmacology

Background:

  • G protein-coupled receptors (GPCRs) are critical drug targets, involved in diverse physiological processes.
  • While structural data from X-ray crystallography and cryo-EM are abundant, they often represent static snapshots.
  • GPCRs are known to be structurally dynamic, exchanging between multiple conformations critical for their function.

Purpose of the Study:

  • To investigate the conformational dynamics of GPCRs using solution Nuclear Magnetic Resonance (NMR) spectroscopy.
  • To elucidate the role of conformational exchange in GPCR signaling mechanisms.
  • To characterize the dynamics of the β2 adrenergic receptor and adenosine A2A receptor.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study GPCRs.
  • Methodological advancements enabled the observation of NMR signals from inherently unstable GPCRs.
  • Studies were conducted in aqueous solutions at near-physiological temperatures.

Main Results:

  • NMR studies revealed that GPCRs exist in dynamic equilibria between distinct, simultaneously populated conformations.
  • These conformational ensembles are directly related to receptor function and signaling.
  • Specific insights into the dynamics of the β2 adrenergic receptor and adenosine A2A receptor were obtained.

Conclusions:

  • Solution NMR is a powerful technique for characterizing the dynamic nature of GPCRs.
  • GPCR function is intrinsically linked to their ability to populate multiple conformations.
  • Understanding these dynamics is essential for developing novel therapeutics targeting GPCRs.