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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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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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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.
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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
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Related Experiment Video

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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Structure network analysis to gain insights into GPCR function.

Francesca Fanelli1, Angelo Felline2, Francesco Raimondi2

  • 1Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125 Modena, Italy fanelli@unimo.it.

Biochemical Society Transactions
|April 13, 2016
PubMed
Summary
This summary is machine-generated.

Protein structure network analysis reveals how G protein coupled receptors (GPCRs) communicate. This method highlights changes in rhodopsin

Keywords:
G protein coupled receptors (GPCRs)elastic network model-normal mode analysismolecular dynamics simulationsprotein structure networksstructural communication

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • G protein coupled receptors (GPCRs) are crucial allosteric proteins mediating cellular signaling.
  • Understanding structural communication within GPCRs is key to their function.
  • Protein structure network (PSN) analysis offers a graph theory-based approach to study biomolecular systems.

Purpose of the Study:

  • To review the application of PSN analysis in uncovering structural communication within GPCRs.
  • To describe strategies for analyzing changes in GPCR structural communication during processes like misfolding, dimerization, and activation.
  • To focus on the ENM-NMA method applied to rhodopsin's inactive and active states.

Main Methods:

  • Utilizing protein structure network (PSN) analysis.
  • Employing coarse-grained elastic network models (ENM) paired with normal mode analysis (NMA).
  • Applying ENM-NMA to crystallographic structures of rhodopsin in inactive (dark) and active (meta II) states.

Main Results:

  • PSN analysis effectively reveals structural communication pathways in GPCRs.
  • Changes in structural communication networks can be identified during GPCR activation.
  • The retinal chromophore's centrality significantly differs between inactive and active rhodopsin states.

Conclusions:

  • PSN analysis, particularly ENM-NMA, is a powerful tool for investigating GPCR structural dynamics.
  • This approach can differentiate between inactive and active GPCR states by analyzing network properties.
  • Understanding these communication mechanisms is vital for drug discovery and understanding receptor function.