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Related Concept Videos

G Protein-coupled Receptors01:15

G Protein-coupled Receptors

19.7K
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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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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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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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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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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G-protein Coupled Receptors01:21

G-protein Coupled Receptors

134.4K
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: Apr 4, 2026

Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
09:19

Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization

Published on: March 16, 2020

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Investigator-blind discovery of structural elements controlling GPCR function.

Jingjing Ji1, Edward Lyman1,2

  • 1Department of Physics and Astronomy, University of Delaware, Newark, DE 19716, USA.

Biorxiv : the Preprint Server for Biology
|April 3, 2026
PubMed
Summary
This summary is machine-generated.

This study introduces an investigator-blind analysis pipeline for molecular dynamics simulations. The pipeline identifies key protein structural elements, including known microswitches and potentially novel motifs in G-protein coupled receptors.

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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
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Related Experiment Videos

Last Updated: Apr 4, 2026

Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
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Monitoring GPCR-β-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery
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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

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Area of Science:

  • Biophysics
  • Computational Biology
  • Structural Biology

Background:

  • Molecular dynamics simulations generate large datasets, necessitating advanced analysis techniques.
  • Analyzing protein dynamics requires rigorous and reproducible methods to understand mechanisms.

Purpose of the Study:

  • To develop an automated, investigator-blind analysis pipeline for molecular dynamics simulation data.
  • To identify key structural features and conformational changes in proteins, particularly G-protein coupled receptors.

Main Methods:

  • Development of an investigator-blind analysis pipeline.
  • Application of unsupervised clustering on featurized simulation data.
  • Identification of discriminatory input features for cluster identity.

Main Results:

  • The pipeline successfully identified known microswitches in G-protein coupled receptor (GPCR) simulations.
  • Observed conformational changes in identified microswitches correlate with known functional transitions.
  • Discovered two potential novel structural motifs: a kink in transmembrane helix 2 and a coupled TM2-TM3 piston-like motion.

Conclusions:

  • The developed pipeline offers a robust method for analyzing complex molecular dynamics data.
  • The findings provide insights into GPCR mechanisms, highlighting known and novel structural elements.
  • This approach enhances the rigor and reproducibility of molecular dynamics simulation analysis.