Shaw G
University of Florida College of Medicine, Department of Neuroscience, Gainesville 32610, USA.
Bioessays. 1996 Jan;18(1):35-46. doi: 10.1002/bies.950180109.
Pleckstrin homology (PH) domains are a family of compact protein modules defined by sequences of roughly 100 amino acids. These domains are common in vertebrate, Drosophila, C. elegans and yeast proteins, suggesting an early origin and fundamental importance to eukaryotic biology. Many enzymes which have important regulatory functions contain PH domains, and mutant forms of several such proteins are implicated in oncogenesis and developmental disorders. Numerous recent studies show that PH domains bind various proteins and inositolphosphates. Here I discuss PH domains in detail and conclude that they form a versatile family of membrane binding and protein localization modules.
普列克底物蛋白同源（PH）结构域是一类由大约100个氨基酸序列定义的紧密蛋白模块。这些结构域在脊椎动物、果蝇、秀丽隐杆线虫和酵母蛋白中很常见，这表明它们起源较早且对真核生物生物学具有重要意义。许多具有重要调节功能的酶都含有PH结构域，几种此类蛋白的突变形式与肿瘤发生和发育障碍有关。最近的大量研究表明，PH结构域能结合各种蛋白质和肌醇磷酸。在此，我将详细讨论PH结构域，并得出结论：它们构成了一个多功能的膜结合和蛋白质定位模块家族。
