Integrative approach for computationally inferring protein domain interactions

Integrative approach for computationally inferring protein domain interactions
复制标题

DOI:
10.1093/bioinformatics/btg118
复制
发表时间:
2003-05-22
期刊:
影响因子:
5.8
通讯作者:
Tan, SH
Tan, SH
中科院分区:
生物学3区
文献类型:
--
作者:
Ng, SK;Zhang, Z;Tan, SH

文献摘要

被引文献

相似文献

动机:目前对高通量蛋白质相互作用检测的需求导致了通过酵母双杂交和蛋白质芯片等实验方法不断产生相互作用数据。这样的数据可能是错误的,并且它们通常不能为检测到的相互作用提供足够的功能信息。因此,它是有用的,以开发一个在硅片上的方法来进一步验证和注释检测到的蛋白质interactions.Results:鉴于蛋白质-蛋白质相互作用涉及蛋白质结构域之间的物理相互作用,结构域-结构域相互作用信息可以是有用的验证,注释,甚至预测蛋白质相互作用。然而,大规模的,实验确定的域域相互作用的数据并不存在。在这里,我们描述了一个综合的方法来计算来自多个数据源,包括蛋白质相互作用,蛋白质复合物,和罗塞塔石碑序列推定的结构域相互作用。我们进一步证明了这样一个综合的方法的有用性,通过应用衍生结构域相互作用来预测和验证蛋白质-蛋白质相互作用。
Motivation: The current need for high-throughput protein interaction detection has resulted in interaction data being generated en masse through such experimental methods as yeast-two-hybrids and protein chips. Such data can be erroneous and they often do not provide adequate functional information for the detected interactions. Therefore, it is useful to develop an in silico approach to further validate and annotate the detected protein interactions.Results: Given that protein-protein interactions involve physical interactions between protein domains, domain-domain interaction information can be useful for validating, annotating, and even predicting protein interactions. However, large-scale, experimentally determined domain-domain interaction data do not exist. Here, we describe an integrative approach to computationally derive putative domain interactions from multiple data sources, including protein interactions, protein complexes, and Rosetta Stone sequences. We further prove the usefulness of such an integrative approach by applying the derived domain interactions to predict and validate protein-protein interactions.