Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex
Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex
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DOI：
10.1016/s1074-5521(00)00078-8
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发表时间：
2000-02-01
影响因子：
--
通讯作者：
Clardy, J
中科院分区：
文献类型：
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作者：
Sandler, BH;Nikonova, L;Clardy, J
背景：昆虫利用挥发性有机分子以极高的敏感性和特异性传递信息。在研究最为深入的系统之一中，雌性家蚕蛾（Bombyx mori）利用信息素蚕蛾醇（一种挥发性的16碳醇）吸引雄性配偶。在雄性蛾的触角中，一种信息素结合蛋白将蚕蛾醇运送至神经细胞上的一种膜结合受体。该信息素结合蛋白的结构、它对蚕蛾醇的结合与识别以及它在信号转导中的全部作用尚不清楚。
结果：结合了蚕蛾醇的家蚕信息素结合蛋白的三维结构已通过X射线衍射在1.8埃分辨率下确定。
结论：家蚕的信息素结合蛋白有6个螺旋，蚕蛾醇结合在一个由4个反平行螺旋形成的完全封闭的疏水腔内。蚕蛾醇通过大量疏水相互作用结合在此腔内，并且序列比对表明了对于特异性信息素结合的关键残基。
Background: Insects use volatile organic molecules to communicate messages with remarkable sensitivity and specificity. In one of the most studied systems, female silkworm moths (Bombyx mori) attract male mates with the pheromone bombykol, a volatile 16-carbon alcohol. In the male moth's antennae, a pheromone-binding protein conveys bombykol to a membrane-bound receptor on a nerve cell. The structure of the pheromone-binding protein, its binding and recognition of bombykol, and its full role in signal transduction are not known.Results: The three-dimensional structure of the B. mori pheromone-binding protein with bound bombykol has been determined by X-ray diffraction at 1.8 Angstrom resolution.Conclusions: The pheromone binding protein of B. mori has six helices, and bombykol binds in a completely enclosed hydrophobic cavity formed by four antiparallel helices. Bombykol is bound in this cavity through numerous hydrophobic interactions, and sequence alignments suggest critical residues for specific pheromone binding.