ArticleNature communications2022
Fusion protein strategies for cryo-EM study of G protein-coupled receptors.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 79 citations in OpenAlex.
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- A novel fusion tool to enable G protein-coupled receptor structure determination.Acta crystallographica. Section D, Structural biology · 2026Article
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- De novo design of GPCR exoframe modulators.Nature · 2026Article
- Designing Rigid Protein Fiducials to Visualize GPCR Conformational States.bioRxiv : the preprint server for biology · 2026Article
- Catalytic Tunnel Dynamics Explain Functional Divergence of FAD2 Homologs Underlying the Oleic-to-Linoleic Ratio inBiology · 2026Article
- Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.Communications biology · 2026Review
- Decoding ligand recognition and constitutive activation of histamine H3 and H4 receptors.Acta pharmacologica Sinica · 2026Article
- Design and Optimization of BRIL Fusion Constructs for Membrane Protein Cryo-EM Studies.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Bottom-up design of CaNature · 2025Article
- Structural insights into the mechanism of activation and inhibition of the prostaglandin D2 receptor 1.Nature communications · 2025Article
- Structural basis for ligand promiscuity and high signaling activity of Kaposi's Sarcoma-associated Herpesvirus-encoded GPCR.Nature communications · 2025Article
- Mechanism and function of GPR3 regulated by a negative allosteric modulator.Nature communications · 2025Article
- De novo design of a fusion protein tool for GPCR research.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure and transport mechanism of human riboflavin transporters.Nature communications · 2025Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Single particle cryogenic-electron microscopy (cryo-EM) is used extensively to determine structures of activated G protein-coupled receptors (GPCRs) in complex with G proteins or arrestins. However, applying it to GPCRs without signaling proteins remains challenging because most receptors lack structural features in their soluble domains to facilitate image alignment. In GPCR crystallography, inserting a fusion protein between transmembrane helices 5 and 6 is a highly successful strategy for crystallization. Although a similar strategy has the potential to broadly facilitate cryo-EM structure determination of GPCRs alone without signaling protein, the critical determinants that make this approach successful are not yet clear. Here, we address this shortcoming by exploring different fusion protein designs, which lead to structures of antagonist bound A
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