A new side to ubiquitin

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• 作者：Camilla Raiborg ; Thomas Slagsvold and Harald Stenmark
• 刊名：Trends in Biochemical Sciences
• 出版年：2006
• 出版时间：October 2006
• 年：2006
• 卷：31
• 期：10
• 页码：541-544
• 全文大小：266 K

文摘

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.