A fast method to predict protein interaction sites from sequences
A fast method to predict protein interaction sites from sequences
复制标题
DOI：
10.1006/jmbi.2000.4092
复制
发表时间：
2000-09-29
影响因子：
5.6
通讯作者：
Brasseur, R
中科院分区：
文献类型：
--
作者：
Gallet, X;Charloteaux, B;Brasseur, R
提出了一种预测蛋白质相互作用位点残基的简单方法。在没有任何结构报告的情况下，该程序通过分析疏水性分布将线性序列段鉴定为“受体结合结构域”（RBD）。测试了引发各种生物活性的非同源相互作用位点的两个数据库的序列; 59- 80%被检测为RBD。在已知的相互作用位点和预测的RBD中进行氨基酸频率的统计分析。从Swissprot数据库的80，000个序列预测RBD。在这两种情况下，精氨酸是最常见的残基。RBD程序还可以检测涉及特定相互作用位点的残基，例如DNA结合域（95%检出）和Ca结合域（83%检出）。我们报告两个最近的分析，从预测的RBD序列的功能活动的实验演示。这些例子涉及逆转录病毒Gag蛋白和青霉素结合蛋白。我们支持这种方法是一种快速的方法来预测蛋白质相互作用位点的序列，并有助于指导实验，如位点特异性诱变，双杂交系统或抑制剂的合成。(C)北京大学出版社.
A simple method for predicting residues involved In protein interaction sites is proposed. In the absence of any structural report, the procedure identifies linear stretches of sequences as "receptor-binding domains" (RBDs) by analysing hydrophobicity distribution. The sequences of two databases of non-homologous interaction sites eliciting various biological activities were tested; 59-80 % were detected as RBDs. A statistical analysis of amino acid frequencies was carried out in known interaction sites and in predicted RBDs. RBDs were predicted from the 80,000 sequences of the Swissprot database. In both cases, arginine is the most frequently occurring residue. The RBD procedure can also detect residues involved in specific interaction sites such as the DNA-binding (95 % detected) and Ca-binding domains (83 % detected). We report two recent analyses; from the prediction of RBDs in sequences to the experimental demonstration of the functional activities. The examples concern a retroviral Gag protein and a penicillin-binding protein. We support that this method is a quick way to predict protein interaction sites from sequences and is helpful for guiding experiments such as site-specific mutageneses, two-hybrid systems or the synthesis of inhibitors. (C) 2000 Academic Press.