Rigden Daniel J
School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, UK.
FEBS Lett. 2004 Jul 2;569(1-3):229-34. doi: 10.1016/j.febslet.2004.05.071.
In eukaryotes some surface proteins are attached to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. A GPI-specific phospholipase D (GPI-PLD) activity has been characterized and implicated in the regulation of anchoring, thereby influencing the dispersal of anchored proteins or their maintenance on the cell surface, and possibly in cell signalling. Despite its biological and medical importance, little is known of the structure of GPI-PLD. Here, a distant relationship between the catalytic domains of GPI-PLD and some bacterial phospholipases C is demonstrated. A model of the GPI-PLD catalytic site sheds light on catalysis and highlights possibilities for design of improved and more specific GPI-PLD inhibitors. The databases contain hitherto unnoticed close homologues of GPI-PLD from yeast and Dictyostelium discoideum.
在真核生物中，一些表面蛋白通过糖基磷脂酰肌醇（GPI）锚定连接到质膜上。一种GPI特异性磷脂酶D（GPI-PLD）活性已被鉴定出来，并与锚定调节有关，从而影响锚定蛋白的分散或它们在细胞表面的维持，还可能参与细胞信号传导。尽管其在生物学和医学上具有重要意义，但对GPI-PLD的结构却知之甚少。在这里，证明了GPI-PLD的催化结构域与一些细菌磷脂酶C之间存在远缘关系。GPI-PLD催化位点的模型揭示了催化过程，并突出了设计改进的、更具特异性的GPI-PLD抑制剂的可能性。数据库中包含来自酵母和盘基网柄菌的迄今未被注意到的GPI-PLD紧密同源物。
