Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM.

Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM.
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DOI:
10.1038/nprot.2011.367
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发表时间:
2011-08-11
期刊:
影响因子:
14.8
通讯作者:
Keskin O
Keskin O
中科院分区:
生物学1区
文献类型:
--
作者:
Tuncbag N;Gursoy A;Nussinov R;Keskin O

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在蛋白质组规模上在结构水平上预测蛋白质-蛋白质相互作用是重要的,因为它允许预测蛋白质功能,有助于药物发现,并向全基因组结构系统生物学迈进。我们提供了一个协议(称为PRISM,蛋白质相互作用的结构匹配)的大规模预测蛋白质-蛋白质相互作用和蛋白质复合物结构的组装。该方法由两个部分组成:刚体结构的目标蛋白质的比较,已知的模板蛋白质-蛋白质界面和灵活的细化使用对接能量函数。PRISM的基本原理遵循我们的观察,即全球不同的蛋白质结构可以通过相似的结构基序相互作用。PRISM预测结合残基通过使用结构相似性和进化保守的推定结合残基的“热点”。最终,PRISM可以帮助构建细胞通路和功能,蛋白质组规模的注释。PRISM在Python中实现,并在UNIX环境中运行。
Prediction of protein-protein interactions at the structural level on the proteome scale is important because it allows prediction of protein function, helps drug discovery and takes steps toward genome-wide structural systems biology. We provide a protocol (termed PRISM, protein interactions by structural matching) for large-scale prediction of protein-protein interactions and assembly of protein complex structures. The method consists of two components: rigid-body structural comparisons of target proteins to known template protein-protein interfaces and flexible refinement using a docking energy function. The PRISM rationale follows our observation that globally different protein structures can interact via similar architectural motifs. PRISM predicts binding residues by using structural similarity and evolutionary conservation of putative binding residue ‘hot spots’. Ultimately, PRISM could help to construct cellular pathways and functional, proteome-scale annotation. PRISM is implemented in Python and runs in a UNIX environment.
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