分离酶的结构域结构及其与securin的结合。

Nature structural & molecular biology Pub Date : 2005-06-01 Epub Date: 2005-05-08 DOI:10.1038/nsmb935
Hector Viadiu, Olaf Stemmann, Marc W Kirschner, Thomas Walz
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引用次数: 51

摘要

分离酶在其抑制剂securin降解后,通过裂解黏结蛋白,在中期到后期转变过程中启动染色体分离。在这里,我们以25a的分辨率呈现了负染色分离-安全复合物的密度图。基于标记数据和序列分析,我们提出了分离酶的结构模型,该模型由26个ARM重复序列,280个残基的非结构化区域和两个caspase样结构域组成,并与ARM重复序列结合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Domain structure of separase and its binding to securin as determined by EM.

After the degradation of its inhibitor securin, separase initiates chromosome segregation during the metaphase-to-anaphase transition by cleaving cohesin. Here we present a density map at a resolution of 25 A of negatively stained separase-securin complex. Based on labeling data and sequence analysis, we propose a model for the structure of separase, consisting of 26 ARM repeats, an unstructured region of 280 residues and two caspase-like domains, with securin binding to the ARM repeats.

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