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相互作用组中同源蛋白质间相互作用的过度呈现。

Overrepresentation of interactions between homologous proteins in interactomes.

作者信息

Orlowski Jerzy, Kaczanowski Szymon, Zielenkiewicz Piotr

机构信息

Laboratory of Plant Molecular Biology, Faculty of Biology, Warsaw University, Pawinskiego 5a, 02-106 Warszawa, Poland.

出版信息

FEBS Lett. 2007 Jan 9;581(1):52-6. doi: 10.1016/j.febslet.2006.11.076. Epub 2006 Dec 8.

Abstract

It is well proved that the probability that a protein interacts with itself is higher than that it interacts with another protein. It has been recently shown that the probability of interaction is also higher for proteins with significant sequence similarity. In this paper we show that proteins sharing identical PFAM domains interact more often than expected by chance in Saccharomyces cerevisiae and Escherichia coli. We also analyze the variety of domain interfaces used by homologous proteins to interact and show that the overrepresentation of interactions between homological proteins is not caused by small number of pairs of identical "sticky domains" shared between interacting proteins.

摘要

充分证明,一种蛋白质与自身相互作用的概率高于它与另一种蛋白质相互作用的概率。最近研究表明,具有显著序列相似性的蛋白质之间的相互作用概率也更高。在本文中,我们表明,在酿酒酵母和大肠杆菌中,共享相同PFAM结构域的蛋白质相互作用的频率比随机预期的更高。我们还分析了同源蛋白质用于相互作用的结构域界面的多样性,并表明同源蛋白质之间相互作用的过度表现并非由相互作用蛋白质之间共享的少量相同“粘性结构域”对所致。

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