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Related Concept Videos

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.
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...
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...
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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GRIPDB - G protein coupled Receptor Interaction Partners DataBase.

Wataru Nemoto1, Kazuhiko Fukui, Hiroyuki Toh

  • 1Computational Biology Research Center (CBRC), Advanced Industrial Science and Technology (AIST), AIST Tokyo, Japan. w.nemoto@aist.go.jp

Journal of Receptor and Signal Transduction Research
|March 18, 2011
PubMed
Summary

G protein-coupled receptors (GPCRs) function as dimers, not monomers. The GRIPDB database compiles experimental and predicted GPCR oligomerization data, aiding research into their signaling mechanisms.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Pharmacology
  • Bioinformatics

Background:

  • G protein-coupled receptors (GPCRs) are crucial pharmaceutical targets, traditionally studied as monomers.
  • Emerging evidence indicates GPCRs frequently form homo- and hetero-oligomers, influencing their function.
  • Understanding GPCR oligomerization is key to elucidating their signaling pathways.

Purpose of the Study:

  • To develop a comprehensive database, GRIPDB, for GPCR oligomerization information.
  • To consolidate experimentally identified GPCR oligomers and their interaction interfaces.
  • To integrate computationally predicted oligomerization interfaces to expand available data.

Main Methods:

  • Database development for storing GPCR oligomerization data.
  • Inclusion of experimentally validated GPCR oligomer information.
  • Application of computational methods for predicting GPCR oligomerization interfaces.

Main Results:

  • The GRIPDB database now provides access to GPCR oligomerization data.
  • Includes experimentally identified GPCR oligomers and suggested interaction interfaces.
  • Features computationally predicted interfaces, visualized using 3D graphics.

Conclusions:

  • GRIPDB facilitates the investigation of GPCR oligomerization mechanisms.
  • The database aids in understanding signal transduction pathways involving GPCR complexes.
  • GRIPDB serves as a valuable resource for GPCR research and drug discovery.