G-protein-coupled receptors (GPCRs) constitute a prominent superfamily in humans, and are categorized into six classes (A through F) that play indispensable roles in cellular communication and therapeutics. Nonetheless, their structural comprehension has been limited by challenges in high-resolution data acquisition. This review highlights the transformative impact of cryogenic electron microscopy (cryo-EM) in the structural determinations of GPCR-G-protein complexes. Specific technologies such as nanobodies and mini-G-proteins stabilize complexes and facilitate structural determination. We discuss the structural alterations upon receptor activation in different GPCR classes, revealing their diverse mechanisms. These cryo-EM structures provide a robust foundation for comprehending GPCR function and pave the way for future breakthroughs in drug discovery and therapeutic targeting.

中文翻译：

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冷冻电镜在 GPCR 结构测定方面的进展

G蛋白偶联受体（GPCR）构成了人类中一个重要的超家族，分为六类（A至F），在细胞通讯和治疗中发挥着不可或缺的作用。尽管如此，他们的结构理解受到高分辨率数据采集挑战的限制。本综述强调了低温电子显微镜 (cryo-EM) 在 GPCR-G 蛋白复合物结构测定中的变革性影响。纳米抗体和迷你 G 蛋白等特定技术可稳定复合物并促进结构确定。我们讨论了不同 GPCR 类别中受体激活时的结构变化，揭示了它们的不同机制。这些冷冻电镜结构为理解 GPCR 功能提供了坚实的基础，并为药物发现和治疗靶向的未来突破铺平了道路。