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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
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...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Monitoring GPCR-&#946;-arrestin1/2 Interactions in Real Time Living Systems to Accelerate Drug Discovery
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GRIP: a server for predicting interfaces for GPCR oligomerization.

Wataru Nemoto1, Kazuhiko Fukui, Hiroyuki Toh

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

Journal of Receptor and Signal Transduction Research
|November 6, 2009
PubMed
Summary
This summary is machine-generated.

Predicting G-Protein Coupled Receptor (GPCR) oligomerization interfaces is challenging. A new web service, GRIP, accurately predicts these interfaces, aiding research into GPCR function and drug development.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • G-Protein Coupled Receptors (GPCRs) are crucial pharmaceutical targets.
  • GPCRs form homo- and hetero-oligomers, but mechanisms remain unclear due to limited structural data.
  • Accurate prediction of GPCR oligomerization interfaces is vital for understanding signaling and developing therapeutics.

Purpose of the Study:

  • To develop a reliable method for predicting GPCR oligomerization interfaces.
  • To address the challenge of varying interface regions across GPCR subtypes.
  • To provide a publicly accessible web service for GPCR interface prediction.

Main Methods:

  • Development of a novel computational method for predicting GPCR oligomerization interfaces.
  • Validation of the method's accuracy across diverse GPCR subtypes.
  • Implementation of the prediction method into a user-friendly web service.

Main Results:

  • The developed method successfully predicts GPCR oligomerization interfaces, overcoming subtype-specific variations.
  • A web service, GRIP (G-protein coupled Receptors Interaction Partners), has been launched.
  • GRIP is currently the only available service for predicting GPCR oligomerization interfaces.

Conclusions:

  • Accurate interface prediction accelerates research into GPCR oligomerization mechanisms and signaling.
  • The GRIP web service provides a valuable tool for the scientific community.
  • This resource facilitates the study of GPCRs as pharmaceutical targets.