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G Protein-coupled Receptors

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 Receptors

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 Proteins

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...

G-protein Coupled Receptors

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 Receptors

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.

GPCR Desensitization

GPCR Desensitization

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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Updated: Jun 8, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Class A GPCR heterodimers: evidence from binding studies.

Nigel J M Birdsall¹

¹Division of Physical Biochemistry, MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK. nbirdsa@nimr.mrc.ac.uk

Trends in Pharmacological Sciences

|September 28, 2010

Summary

G protein-coupled receptor (GPCR) heterodimers may have unique functions. This review explores evidence for allosteric interactions within GPCR heterodimers, suggesting more data is needed to confirm cross-receptor binding modulation.

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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

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Last Updated: Jun 8, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Published on: October 8, 2015

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

Area of Science:

Pharmacology
Molecular Biology
Biochemistry

Background:

G protein-coupled receptors (GPCRs) form heterodimers with distinct functional properties.
The existence and functional implications of GPCR heterodimers are supported by substantial experimental evidence.
A key question is whether receptor-receptor interactions within heterodimers cause allosteric modulation of binding and pharmacology.

Purpose of the Study:

To review experimental evidence regarding allosteric interactions in GPCR heterodimers.
To analyze radioligand binding studies in the context of various allosterism models.
To discuss discrepant results and their implications for understanding GPCR heterodimer function.

Main Methods:

Review of published experimental data, primarily from radioligand binding studies.
Analysis of findings within theoretical frameworks of allosterism.
Discussion of conflicting experimental outcomes.

Main Results:

Existing evidence is compatible with GPCR heterodimer formation.
The presence of allosteric interactions modulating binding properties requires further investigation.
Discrepant results highlight the complexity of studying GPCR heterodimer pharmacology.

Conclusions:

GPCR heterodimers are plausible and may possess unique functional characteristics.
Unequivocal demonstration of equal, two-way allosteric interactions at the binding level requires more experimental data.
Further research is essential to fully elucidate the mechanisms and consequences of GPCR heterodimerization.