Structural features of activated GPCR signaling complexes
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Updated: Dec 20, 2025

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
Jingjing Wang1, Tian Hua2, Zhi-Jie Liu1
1iHuman Institute, ShanghaiTech University, Shanghai 201210, China; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
Abstract:
G protein-coupled receptors (GPCRs) couple to diverse heterotrimeric G protein subtypes and then activate downstream signaling pathways in classical GPCR activation. It has also been found that GPCRs transduce signals through different regulatory proteins, such as arrestins. Recently, owing to the breakthroughs in cryo-electron macroscopy (Cryo-EM), numerous structures of GPCR-G protein or GPCR-arrestin complexes have been deciphered. In this review, we summarize most of reported GPCR signaling complex structures, with an emphasis on the structural features of rhodopsin-like GPCR activation and G protein-binding/arrestin-binding modes, to illustrate the activation and signaling mechanism of rhodopsin-like GPCRs.
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