环形变化：不同泛素和泛素样蛋白对 Parkin 活性的调控

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure Pub Date : 2024-11-07 DOI:10.1016/j.str.2024.10.015

Shalini Iyer, Chittaranjan Das

引用次数: 0

摘要

在激酶 PINK1 的介导下，泛素和 Parkin 的泛素样结构域发生磷酸化是 E3 连接酶从自身抑制状态中解放出来的必要条件。在本期《结构》杂志上，Lenka 等人1 提供了磷酸化 NEDD8 与磷酸化泛素相比具有特异性和更强的 Parkin 激活的结构基础。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Ringing the changes: Regulation of Parkin activity by different ubiquitin and ubiquitin-like proteins

Phosphorylation of ubiquitin and the ubiquitin-like domain of Parkin, mediated by the kinase PINK1, is essential for the liberation of the E3 ligase from its autoinhibited state. In this issue of Structure, Lenka et al.¹ provide the structural basis for the specificity and stronger Parkin activation by phospho-NEDD8 compared to phospho-ubiquitin.

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来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.