De novo Design of A Fusion Protein Tool for GPCR Research

Kaixuan Gao, Xin Zhang, Jia Nie, Hengyu Meng, Weishe Zhang, Boxue Tian, Xiangyu Liu
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Abstract

G protein-coupled receptors (GPCRs) play pivotal roles in cellular signaling and represent prominent drug targets. Structural elucidation of GPCRs is crucial for drug discovery efforts. However, structural studies of GPCRs remain challenging, particularly for inactive state structures, which often require extensive protein engineering. Here, we present a de novo design strategy termed "click fusion" for generating fusion proteins to facilitate GPCR structural studies. Our method involves the rational design of structurally stable protein domains rigidly linked to GPCRs. The resulting fusion protein enhances the thermostability of the target GPCR and aids in determining GPCR structures via cryo-electron microscopy (cryo-EM). We further demonstrate that the designed fusion protein can be transferred among structurally similar GPCRs with minor adjustments to the linker region. Our study introduces a promising approach for facilitating GPCR structural studies and advancing drug discovery efforts.
从头设计用于 GPCR 研究的融合蛋白工具
G 蛋白偶联受体(GPCR)在细胞信号传导中起着关键作用,是重要的药物靶点。阐明 GPCR 的结构对药物发现工作至关重要。然而,GPCR 的结构研究仍然具有挑战性,尤其是非活性状态结构的研究,这通常需要大量的蛋白质工程。在这里,我们提出了一种称为 "点击融合 "的全新设计策略,用于生成融合蛋白以促进 GPCR 结构研究。我们的方法包括合理设计与 GPCR 刚性连接的结构稳定的蛋白质结构域。由此产生的融合蛋白可提高目标 GPCR 的热稳定性,并有助于通过冷冻电镜(cryo-EM)确定 GPCR 结构。我们进一步证明,只需对连接区稍作调整,设计的融合蛋白就能在结构相似的 GPCR 之间转移。我们的研究为促进 GPCR 结构研究和推进药物发现工作引入了一种前景广阔的方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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