Identification of transient hub proteins and the possible structural basis for their multiple interactions
Identification of transient hub proteins and the possible structural basis for their multiple interactions
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DOI：
10.1110/ps.073196308
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发表时间：
2008-01-01
期刊：
影响因子：
8
通讯作者：
Kinoshita, Kengo
中科院分区：
文献类型：
--
作者：
Higurashi, Miho;Ishida, Takashi;Kinoshita, Kengo
能够与多个伴侣相互作用的蛋白质在蛋白质-蛋白质相互作用网络中起着核心作用。它们被称为枢纽蛋白，最近有人提出，它们表面上丰富的内在无序区域有助于它们与多个伴侣结合。然而，在这些研究中，枢纽蛋白被鉴定为具有多个伴侣的蛋白质，无论相互作用是短暂的还是永久的。因此，一定数量的枢纽蛋白是稳定的多亚基蛋白的亚基，例如超分子。稳定复合物和瞬时复合物具有不同的结构特征，因此基于目前对枢纽蛋白定义的统计将掩盖枢纽蛋白的真实性质。因此，在本文中，我们首先描述了一种新的方法来确定蛋白质与多个合作伙伴的动态，使用蛋白质数据库，然后我们进行了统计分析，这些蛋白质的结构特征。我们将这些蛋白质称为瞬时枢纽蛋白或社交蛋白，以阐明与枢纽蛋白的区别。结果，我们发现，与以前的研究相反，社会性和非社会性蛋白质之间的主要区别不是无序区域的丰富程度，而是整个蛋白质的结构灵活性。我们还发现更大的优势，带电和极性残基的社会性蛋白质比以前报道的。
Proteins that can interact with multiple partners play central roles in the network of protein-protein interactions. They are called hub proteins, and recently it was suggested that an abundance of intrinsically disordered regions on their surfaces facilitates their binding to multiple partners. However, in those studies, the hub proteins were identified as proteins with multiple partners, regardless of whether the interactions were transient or permanent. As a result, a certain number of hub proteins are subunits of stable multi- subunit proteins, such as supramolecules. It is well known that stable complexes and transient complexes have different structural features, and thus the statistics based on the current definition of hub proteins will hide the true nature of hub proteins. Therefore, in this paper, we first describe a new approach to identify proteins with multiple partners dynamically, using the Protein Data Bank, and then we performed statistical analyses of the structural features of these proteins. We refer to the proteins as transient hub proteins or sociable proteins, to clarify the difference with hub proteins. As a result, we found that the main difference between sociable and nonsociable proteins is not the abundance of disordered regions, in contrast to the previous studies, but rather the structural flexibility of the entire protein. We also found greater predominance of charged and polar residues in sociable proteins than previously reported.