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Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gβ5 signaling complex
Science ( IF 44.7 ) Pub Date : 2022-01-06 , DOI: 10.1126/science.abl4732
Dipak N Patil 1 , Shikha Singh 2 , Thibaut Laboute 1 , Timothy S Strutzenberg 3 , Xingyu Qiu 4, 5 , Di Wu 4, 5 , Scott J Novick 3 , Carol V Robinson 4, 5 , Patrick R Griffin 3 , John F Hunt 2 , Tina Izard 6 , Appu K Singh 7, 8 , Kirill A Martemyanov 1
Affiliation  

Not your typical GPCR Among the large family of G protein–coupled receptors (GPCRs) are many orphans, so called because their signaling reactions remain poorly understood. Among these is GPR158 which is highly expressed in the nervous system and implicated in processes from cognition to memory to mood. Patil et al . determined a high-resolution structure of GPR158 alone and bound to a regulator of G protein signaling (RGS) complex. GPR158 has an unusual dimerization mode with an extensive interaction interface that locks it in a conformation that likely prevents G protein activation. RGS binds to the homodimer at a site that substantially overlaps the surface that binds G proteins, again preventing canonical G protein signaling. Binding of a ligand to the extracellular domain may regulate signaling through the RGS complex. —VV

中文翻译:

人 GPR158 受体与 RGS7-Gβ5 信号复合物耦合的低温电子显微镜结构

不是典型的 GPCR 在 G 蛋白偶联受体 (GPCR) 的大家族中有许多孤儿,之所以这样称呼是因为它们的信号反应仍然知之甚少。其中包括 GPR158,它在神经系统中高度表达,并涉及从认知到记忆再到情绪的过程。帕蒂尔等人. 单独确定了 GPR158 的高分辨率结构,并与 G 蛋白信号转导 (RGS) 复合物的调节剂结合。GPR158 具有不寻常的二聚化模式,具有广泛的相互作用界面,可将其锁定在可能阻止 G 蛋白激活的构象中。RGS 在与结合 G 蛋白的表面基本重叠的位点与同型二聚体结合,再次阻止典型的 G 蛋白信号传导。配体与细胞外结构域的结合可以调节通过 RGS 复合体的信号传导。—VV
更新日期:2022-01-06
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