泛素识别中的结构复杂性
Structural complexity in ubiquitin recognition.
作者信息
Harper J Wade, Schulman Brenda A
机构信息
Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.
出版信息
Cell. 2006 Mar 24;124(6):1133-6. doi: 10.1016/j.cell.2006.03.009.
PMID:16564007
Abstract
Ubiquitinated proteins are sorted into distinct pathways via association with several classes of ubiquitin binding domain-containing proteins. A virtual explosion in the field of ubiquitin binding proteins has revealed several new classes and interactions with distinct surfaces on ubiquitin, providing a clearer understanding of how sorting of ubiquitinated proteins is achieved.
摘要
泛素化蛋白通过与几类含泛素结合结构域的蛋白结合，被分选到不同的途径中。泛素结合蛋白领域的一场实质意义上的“爆炸”揭示了几个新的类别以及与泛素不同表面的相互作用，这让人们对泛素化蛋白的分选是如何实现的有了更清晰的理解。
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