HERC2 E3 泛素连接酶 ZZ 结构域的生化分析和结构测定方案。
Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2.
机构信息
Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Center for Epigenetics, Van Andel Research Institute, Grand Rapids, MI 49503, USA.
出版信息
STAR Protoc. 2020 Oct 28;1(3):100155. doi: 10.1016/j.xpro.2020.100155. eCollection 2020 Dec 18.
Since its discovery, several ligands of the ZZ domain have been identified; however, molecular and structural information underlying binding of these ligands remains limited. Here, we describe a protocol for biochemical and structural analysis of the ZZ domain of human E3 ubiquitin ligase HERC2 (HERC2) and its interaction with its ligands: the N-terminal tails of histone H3 and SUMO1. This methodology could be applied for characterization of binding activities of other histone readers. For complete details on the use and execution of this protocol, please refer to Liu et al. (2020).
自发现以来，已经鉴定出 ZZ 结构域的几种配体；然而，这些配体结合的分子和结构信息仍然有限。在这里，我们描述了一种用于生化和结构分析人 E3 泛素连接酶 HERC2（HERC2）的 ZZ 结构域及其与配体相互作用的方案：组蛋白 H3 的 N 端尾巴和 SUMO1。该方法可用于表征其他组蛋白阅读器的结合活性。有关该方案的使用和执行的完整详细信息，请参阅 Liu 等人。（2020 年）。
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