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Crystallization and preliminary X-ray crystallographic study of the human MST2 SARAH domain.人MST2 SARAH结构域的结晶及初步X射线晶体学研究
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Importin alpha protein acts as a negative regulator for Snail protein nuclear import.Importin alpha 蛋白作为 Snail 蛋白核内输入的负调节剂起作用。
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人输入蛋白β-蜗牛锌指结构域复合物的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of human importin β-Snail zinc finger domain complex.

作者信息

Choi Saehae, Song Jinsue, Son Se-Young, Park Il Yeong, Yamashita Eiki, Lee Soo Jae

机构信息

College of Pharmacy, Chungbuk National University, 410 Seungbong, Heungduk, Cheongju 361-763, Republic of Korea.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):1049-51. doi: 10.1107/S1744309113023038. Epub 2013 Aug 23.

DOI:10.1107/S1744309113023038
PMID:23989161
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3758161/
Abstract

Snail is a C2H2-type zinc finger transcriptional repressor that induces epithelial-mesenchymal transition by repression of E-cadherin expression levels during embryonic development and tumour progression. Snail is imported into the nucleus by importin β through direct binding with its four zinc finger domain. The complex between importin β and Snail four zinc finger domain was crystallized in order to understand the nuclear transport mechanism of Snail. The constituents of the complex were separately expressed and were then co-purified and crystallized by the hanging-drop vapour-diffusion method. The crystals belonged to space group C2, with unit-cell parameters a = 228.2, b = 77.5, c = 72.0 Å, β = 100.9° and diffracted to 2.5 Å resolution.

摘要

Snail是一种C2H2型锌指转录抑制因子,在胚胎发育和肿瘤进展过程中,它通过抑制E-钙黏蛋白的表达水平来诱导上皮-间质转化。Snail通过其四个锌指结构域与importin β直接结合,从而被importin β转运到细胞核中。为了了解Snail的核转运机制,对importin β与Snail四个锌指结构域之间的复合物进行了结晶。复合物的组成成分分别表达,然后通过悬滴气相扩散法进行共纯化和结晶。晶体属于空间群C2,晶胞参数为a = 228.2、b = 77.5、c = 72.0 Å,β = 100.9°,衍射分辨率为2.5 Å。