Structural basis of ubiquitylation.
Structural basis of ubiquitylation.
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DOI：
10.1016/s0959-440x(02)00389-5
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发表时间：
2002-12
影响因子：
6.8
通讯作者：
A. Vandemark;C. Hill
中科院分区：
文献类型：
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作者：
A. Vandemark;C. Hill
小蛋白泛素附着到其他蛋白质上，这一过程被称为泛素化，是一种广泛存在的翻译后修饰形式，在真核生物中调节许多细胞功能。泛素化是由E2和E3酶的复合物完成的，这些复合物通过一系列蛋白质-蛋白质相互作用组装并选择底物。最近对泛素化机制的结构测定揭示了涉及的各种蛋白质-蛋白质界面。
The attachment of the small protein ubiquitin to other proteins, a process known as ubiquitylation, is a widespread form of post-translational modification that regulates numerous cellular functions in eukaryotes. Ubiquitylation is performed by complexes of E2 and E3 enzymes that are assembled and select substrates via a series of protein–protein interactions. Recent structure determinations of the ubiquitylation machinery have revealed some of the various protein–protein interfaces involved.