A new side to ubiquitin.
A new side to ubiquitin.
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泛素的新一面。
DOI：
10.1016/j.tibs.2006.07.009
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发表时间：
2006
影响因子：
13.8
通讯作者：
H. Stenmark
中科院分区：
文献类型：
--
作者：
C. Raiborg;Thomas Slagsvold;H. Stenmark
单一泛素化是一种常见的蛋白质调控机制，已有十多个泛素相互作用结构域识别以泛素Ile44为中心的疏水区。最近的两篇报道描述了Rab5鸟嘌呤核苷酸交换因子Rabex-5的晶体结构，并表明它含有两个新的泛素结合域。其中之一是A20锌指，它结合到以Asp58为中心的泛素的极性相互作用界面上。泛素的另一种相互作用面的发现为理解这种小蛋白如何调节蛋白质功能开辟了新的途径。
Mono-ubiquitination is a common mechanism of protein regulation, and more than ten ubiquitin-interacting domains that recognize the hydrophobic region centered on Ile44 of ubiquitin have been characterized. Two recent reports describe the crystal structure of the Rab5 guanine-nucleotide-exchange factor Rabex-5 and show that it contains two novel ubiquitin-binding domains. One of these is an A20 zinc finger that binds to a polar interaction interface of ubiquitin centered on Asp58. The discovery of an alternative interaction face of ubiquitin opens new avenues for understanding how this small protein regulates protein function.
影响因子：
16
作者：
Levkowitz, G;Waterman, H;Yarden, Y
通讯作者：
Yarden, Y