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Scientific rendering of 3D protein structure, structural biology | Nano Imaging
Scientific rendering of 3D protein structure, structural biology | Nano Imaging

G-Protein Coupled Receptors (GPCRs) are the largest class of cell surface receptors that play a central role in transmitting signals from the extracellular environment to the interior of cells. These receptors act as molecular switches, activating intracellular signaling pathways upon binding specific ligand molecules, which can include neurotransmitters, hormones, or other signaling molecules.

The significance of GPCRs in therapeutics stems from their involvement in numerous physiological processes. Due to their role in various diseases, GPCRs are highly attractive targets for drug development. More than 30% of FDA-approved drugs act on 108 unique GPCR targets, and there are over 60 novel GPCR targets currently in clinical trials ( By modulating the activity of GPCRs, drugs can enhance or inhibit their signaling, leading to therapeutic effects. 

Solve your novel GPCR with high resolution cryo-EM imaging.

In the period between 2020 and 2022, more structures of GPCRs have been determined than in the previous two decades, primarily through the use of cryo-EM ( According to research, cryo-EM accounted for 78% of the 99 GPCR structures deposited into the Protein Data Bank (PDB) between January and July 2021. (

While traditional methods such as X-ray crystallography and NMR spectroscopy have been utilized to determine the 3D structures of proteins, GPCRs have posed significant challenges due to their complexity, flexible structures and their propensity to destabilize outside of their native cell membrane environment.

Cryo-EM overcomes most of these limitations and  allows scientists to study GPCRs at near-atomic resolution. This capability is vital for understanding the intricate molecular interactions involved in GPCR activation and signaling.

Ligand binding and interaction with other proteins, such as G-proteins and arrestins, can induce various conformational states in GPCRs. Cryo-EM allows for the capture of these dynamic states, providing valuable insights into the mechanisms of ligand binding and signaling, further enhancing our understanding of GPCR biology.

As the field of cryo-EM and GPCR research advances, the potential for groundbreaking discoveries and the development of highly targeted drugs to address a range of diseases remains promising. 

Contact us to schedule a meeting to discuss how high resolution cryo-EM can help solve your GPCR. 

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Do you have any examples of GPCRs solved with cryo-EM?

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In this paper, New insights into GPCR coupling and dimerisation from cryo-EM structures, by Gusach et al., cryo-EM structures of GPCR dimers have been determined for Class A, C and D receptors, he first GPCR-GRK structure has been determined, arrestin-coupled GPCR structures provide new insights for the development of biased agonists, and methodologies have been developed for determining cryo-EM structures of inactive state GPCRs.

In this paper, Evolving cryo-EM structural approaches for GPCR drug discovery, by Zhang et al., the authors use the PF 06882961-bound GLP-1R and used a 200 kV Glacios-Falcon 4 cryo electron microscope, which yielded a 3.2 Å map with clear density for bound drug and multiple structurally ordered waters. NIS has multiple 200 kV microscopes on our West and East coast labs, and can assist you in solving your GPCR structure.

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