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Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors.

机译:氨基酸共进化揭示了昆虫气味受体的三维结构和功能域。

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摘要

Insect odorant receptors (ORs) comprise an enormous protein family that translates environmental chemical signals into neuronal electrical activity. These heptahelical receptors are proposed to function as ligand-gated ion channels and/or to act metabotropically as G protein-coupled receptors (GPCRs). Resolving their signalling mechanism has been hampered by the lack of tertiary structural information and primary sequence similarity to other proteins. We use amino acid evolutionary covariation across these ORs to define restraints on structural proximity of residue pairs, which permit de novo generation of three-dimensional models. The validity of our analysis is supported by the location of functionally important residues in highly constrained regions of the protein. Importantly, insect OR models exhibit a distinct transmembrane domain packing arrangement to that of canonical GPCRs, establishing the structural unrelatedness of these receptor families. The evolutionary couplings and models predict odour binding and ion conduction domains, and provide a template for rationale structure-activity dissection.
机译:昆虫气味受体(OR)包含一个巨大的蛋白质家族,可将环境化学信号转化为神经元电活动。这些七螺旋受体被提议用作配体门控离子通道和/或作为G蛋白偶联受体(GPCR)代谢型地起作用。由于缺乏三级结构信息和与其他蛋白质的一级序列相似性,阻碍了其信号传导机制的解决。我们使用跨这些OR的氨基酸进化协变来定义对残基对结构邻近性的限制,从而允许从头生成三维模型。我们的分析的有效性得到了蛋白质高度受限区域中功能重要残基的定位的支持。重要的是,昆虫OR模型表现出与经典GPCR截然不同的跨膜结构域排列安排,从而确定了这些受体家族的结构无关性。进化耦合和模型预测气味结合和离子传导域,并为基本结构活性解剖提供模板。

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