Sialidase-like Asp-boxes: Sequence-similar structures within different protein folds
Sialidase-like Asp-boxes: Sequence-similar structures within different protein folds
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DOI：
10.1110/ps.31901
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发表时间：
2001-02-01
期刊：
影响因子：
8
通讯作者：
Ponting, CP
中科院分区：
文献类型：
--
作者：
Copley, RR;Russell, RB;Ponting, CP
序列相似性是当前用于推断蛋白质同源性的最常见措施。通常，同源蛋白结构域在整个长度上显示出序列相似性。在这里，我们在新的结构和序列上下文中识别出在唾液酸酶和神经氨酸酶中重复的ASP盒序列。这些基序代表了明显相似的序列，该序列位于蛋白质中的P发夹，这些序列在序列和三维结构上不同。通过进行基于序列和结构的组合分析，我们检测到超过9种蛋白质家族中的ASP盒，包括细菌核糖珠，亚硫酸盐氧化酶，reelin，Netrins，一些脂蛋白受体和各种糖基水解酶。尽管这些蛋白质中的每一种（如果有的话）仍然不清楚的功能，但我们根据先前确定的实验结果讨论ASP框的可能功能，并讨论了含有ASP-box的蛋白质的起源的不同进化场景。
Sequence similarity is the most common measure currently used to infer homology between proteins. Typically, homologous protein domains show sequence similarity over their entire lengths. Here we identify Asp box motifs, initially found as repeats in sialidases and neuraminidases, in new structural and sequence contexts. These motifs represent significantly similar sequences, localized to P hairpins within proteins that are otherwise different in sequence and three-dimensional structure. By performing a combined sequence-and structure-based analysis we detect Asp boxes in more than nine protein families, including bacterial ribonucleases, sulfite oxidases, reelin, netrins, some lipoprotein receptors, and a variety of glycosyl hydrolases. Although the function common to each of these proteins, if any, remains unclear, we discuss possible functions of Asp boxes on the basis of previously determined experimental results and discuss different evolutionary scenarios for the origin of Asp-box containing proteins.