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The pyrokinin/pheromone biosynthesis-activating neuropeptide (PBAN) family of peptides and their receptors in Insecta: evolutionary trace indicates potential receptor ligand-binding domains

机译:昆虫纲中的丙酮酸激酶/信息素生物合成激活神经肽(PBAN)家族及其受体:进化轨迹表明潜在的受体配体结合域

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摘要

The pyrokinin/pheromone biosynthesis-activating neuropeptide (PBAN) family of G-protein-coupled receptors and their ligands have been identified in various insects. Physiological functions of pyrokinin peptides include muscle contraction, whereas PBAN regulates, among other functions, pheromone production in moths which indicates the pleiotropic nature of these peptides. Based on the alignment of annotated genomic sequences, the pyrokinin/PBAN family of receptors have similarity with the corresponding structures of the capa or periviscerokinin receptors of insects and the neuromedin U receptors of vertebrates. In our study, evolutionary trace (ET) analysis on the insect receptor sequences was conducted to predict the putative ligand recognition and binding sites. The ET analysis of four class-specific receptors indicated several amino acid residues that are conserved in the transmembrane domains. The receptor extracellular domains exhibit several class-specific amino acid residues, which could indicate putative domains for activation of these receptors by ligand recognition and binding.
机译:已经在各种昆虫中鉴定出了G蛋白偶联受体的激动素/信息素生物合成激活神经肽(PBAN)家族。焦磷酸肌动蛋白肽的生理功能包括肌肉收缩,而PBAN除其他功能外还调节飞蛾中信息素的产生,这表明这些肽具有多效性。基于注释的基因组序列的比对,焦磷酸激酶/ PBAN受体家族与昆虫的Capa或膜黏膜活化素受体的相应结构以及脊椎动物的神经调节素U受体具有相似的结构。在我们的研究中,对昆虫受体序列进行了进化痕量(ET)分析,以预测推定的配体识别和结合位点。四种类特异性受体的ET分析表明,跨膜结构域中保守的几个氨基酸残基。受体的细胞外结构域表现出几个类别特异性氨基酸残基,这可能表明通过配体识别和结合激活这些受体的推定结构域。

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