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首页> 外文期刊>Journal of pesticide science >Amino acid residues involved in the interaction with the intrinsic agonist (R)-octopamine in the β-adrenergic-like octopamine receptor from the silkworm Bombyx mori
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Amino acid residues involved in the interaction with the intrinsic agonist (R)-octopamine in the β-adrenergic-like octopamine receptor from the silkworm Bombyx mori

机译：与家蚕的β-肾上腺素样章鱼胺受体中的内在激动剂（R）-章鱼胺相互作用的氨基酸残基

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摘要

Octopamine (OA) is a biogenic amine that controls a variety of important physiological processes and behaviors of invertebrates. To identify the amino acid residues interacting with ( R )-OA in a β-adrenergic-like OA receptor from the silkworm Bombyx mori (BmOAR2), the wild-type receptor and seven mutant receptors with an amino acid substitution at a potential orthosteric site were expressed in HEK-293 cells and examined for their ability to elevate intracellular cAMP levels ([cAMP]i) in response to ( R )-OA. The S206A mutant receptor retained the ability to increase [cAMP]i after ( R )-OA treatment. In contrast, the other six mutant receptors (D115A, S202A, Y300F, Y300N, Y300L, and Y300A) lacked the ability to elevate [cAMP]i. These results indicate that Asp115, Ser202, and Tyr300 participate in ( R )-OA binding and the activation of BmOAR2. Homology modeling studies suggest that Ser202 and Tyr300 interact with the phenolic OH group of ( R )-OA, whereas Asp115 interacts with the β-OH group and the NH2 group of ( R )-OA.
机译：章鱼胺（OA）是一种生物胺，可控制无脊椎动物的各种重要生理过程和行为。为了鉴定与家蚕Bombyx mori（BmOAR2）的β-肾上腺素样OA受体中与（R）-OA相互作用的氨基酸残基，野生型受体和七个突变受体，这些受体在潜在的正构位点被氨基酸取代它们在HEK-293细胞中表达，并检测它们响应（R）-OA升高细胞内cAMP水平（[cAMP] i ）的能力。 S206A突变体受体保留（R）-OA处理后增加[cAMP] i 的能力。相反，其他六个突变受体（D115A，S202A，Y300F，Y300N，Y300L和Y300A）缺乏提高[cAMP] i 的能力。这些结果表明Asp115，Ser202和Tyr300参与（R）-OA结合和BmOAR2的激活。同源模型研究表明，Ser202和Tyr300与（R）-OA的酚羟基相互作用，而Asp115与（R）-OA的β-OH基和NH 2 基相互作用。

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