Lautenschlager Catherine, Leal Walter S, Clardy Jon
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Structure. 2007 Sep;15(9):1148-54. doi: 10.1016/j.str.2007.07.013.
Insect pheromone-binding proteins (PBPs) transport sex pheromones through the aqueous layer surrounding G protein-coupled receptors that initiate signaling events leading to mating. This PBP-receptor system strongly discriminates between ligands with subtle structural differences, but it has proved difficult to distinguish the degree of discrimination of the PBP from that of the G protein-coupled receptor. The three-dimensional structures of the PBP of Bombyx mori, the silkworm moth, both with and without its cognate ligand bombykol ([E,Z]-10,12-hexadecadienol), have been determined by X-ray crystallography and NMR. In this paper, the structures of the same binding protein with bound iodohexadecane and bell pepper odorant were determined at 1.9 and 2.0 A, respectively. These structures illustrate the remarkable plasticity in the ligand binding site of the PBP, but suggest the protein might still act as a filter during pheromone signal processing.
昆虫信息素结合蛋白（PBPs）通过围绕G蛋白偶联受体的水层运输性信息素，这些受体启动导致交配的信号事件。这种PBP-受体系统能强烈区分结构差异细微的配体，但事实证明，很难区分PBP与G蛋白偶联受体的区分程度。家蚕（桑蚕蛾）的PBP在结合和未结合其同源配体蚕蛾醇（[E,Z]-10,12-十六碳二烯醇）的情况下，其三维结构已通过X射线晶体学和核磁共振确定。在本文中，分别在1.9 Å和2.0 Å的分辨率下确定了结合碘代十六烷和甜椒气味剂的同一结合蛋白的结构。这些结构说明了PBP配体结合位点具有显著的可塑性，但表明该蛋白在信息素信号处理过程中可能仍起到筛选作用。
