泛素连接酶E3

Ubiquitin Ligase E3

蛋白质的泛素化修饰具有高度的特异性,它参与调节细胞内许多的生理活动。蛋白质的泛素化修饰涉及一系列的酶参与反应,包括泛素激活酶E1、结合酶E2以及连接酶E3。而其中泛素连接酶E3对靶蛋白的特异性识别起关键作用。泛素连接酶E3主要由HECT结构域家族、RING结构域家族和U-box结构域家族组成。现对泛素连接酶E3的分类、结构及其对靶蛋白的识别机制等进行综述。

Ubiquitination of protein is high selective and very important in regulating various cellular processes. Ubiquitination involves the successive actions of the ubiquin-activating enzyme(E1), ubiquitin-conjugating enzyme(E2), and ubiquitin-protein ligase enzyme(E3). E3 is most directly responsible for substrate recognization. It contains three members, including HECT domain E3, RING domain E3, and U-box domain E3. Here, we summarize the classification, the structure and the mechanism of substrate recognization of ubiquitin-protein ligase enzyme (E3).