ArticleProceedings of the National Academy of Sciences of the United States of America2024
Calcineurin-fusion facilitates cryo-EM structure determination of a Family A GPCR.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A Minimalist Model for Navigating Conformational Landscape Uncovers the Activation Mechanism of βACS physical chemistry Au · 2026Article
- Universal pipeline for high-resolution GPCR structure determination.Nature structural & molecular biology · 2026Article
- A novel fusion tool to enable G protein-coupled receptor structure determination.Acta crystallographica. Section D, Structural biology · 2026Article
- Strategic advances for cryo-EM structural studies of small (<100 kDa) GPCRs.Communications biology · 2026Review
- Mechanism and function of GPR3 regulated by a negative allosteric modulator.Nature communications · 2025Article
- Structure of a lasso peptide bound ETNature communications · 2025Article
- Article
- New insights into GPCR coupling and dimerisation from cryo-EM structures.Current opinion in structural biology · 2023Review
- New Insights into the Structure and Function of Class B1 GPCRs.Endocrine reviews · 2023Article
- The structure, function, and pharmacology of MRGPRs.Trends in pharmacological sciences · 2023Review
- Putting on molecular weight: Enabling cryo-EM structure determination of sub-100-kDa proteins.Current research in structural biology · 2022Review
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Authors and funding
8 authors.
Funding
Abstract
Advances in singe-particle cryo-electron microscopy (cryo-EM) have made it possible to solve the structures of numerous Family A and Family B G protein-coupled receptors (GPCRs) in complex with G proteins and arrestins, as well as several Family C GPCRs. Determination of these structures has been facilitated by the presence of large extramembrane components (such as G protein, arrestin, or Venus flytrap domains) in these complexes that aid in particle alignment during the processing of the cryo-EM data. In contrast, determination of the inactive state structure of Family A GPCRs is more challenging due to the relatively small size of the seven transmembrane domain (7TM) and to the surrounding detergent micelle that, in the absence of other features, make particle alignment impossible. Here, we describe an alternative protein engineering strategy where the heterodimeric protein calcineurin is fused to a GPCR by three points of attachment, the cytoplasmic ends of TM5, TM6, and TM7. This three-point attachment provides a more rigid link with the GPCR transmembrane domain that facilitates particle alignment during data processing, allowing us to determine the structures of the β
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