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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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Activation and Inactivation of G Proteins01:22

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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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Transducer Mechanism: G Protein–Coupled Receptors01:30

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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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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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G-protein Coupled Receptors01:21

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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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Related Experiment Video

Updated: Mar 16, 2026

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
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Cholesterol-dependent Conformational Plasticity in GPCR Dimers.

Xavier Prasanna1, Durba Sengupta1, Amitabha Chattopadhyay2

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Cholesterol increases the flexibility of serotonin1A receptor dimers by affecting their interface. This finding clarifies the molecular mechanism of cholesterol-dependent GPCR organization and may inform drug development.

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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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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Serotonin1A receptor, a G protein-coupled receptor (GPCR), exhibits cholesterol-dependent organization and function.
  • The precise molecular mechanisms underlying this cholesterol dependency remain unclear.

Purpose of the Study:

  • To comprehensively analyze the structural and dynamic aspects of serotonin1A receptor dimerization.
  • To elucidate the molecular details of cholesterol-dependent association in this GPCR.

Main Methods:

  • Utilized coarse-grain molecular dynamics simulations.
  • Simulations totaled 3.6 milliseconds to capture receptor dynamics.
  • Focused on structural and dynamic analysis of receptor dimerization.

Main Results:

  • Increased cholesterol concentration correlated with enhanced plasticity and flexibility of receptor dimers.
  • A specific dimer interface involving transmembrane helices I-I demonstrated cholesterol sensitivity.
  • Cholesterol's influence on the dimer interface arises from direct occupancy and indirect membrane effects.

Conclusions:

  • Cholesterol directly modulates serotonin1A receptor dimer plasticity and flexibility.
  • Findings provide molecular insights into cholesterol-GPCR interactions.
  • These results have potential implications for therapeutic strategies targeting GPCRs.