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

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

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1
College of Pharmacy, Chungbuk National University, 410 Seungbong, Heungduk, Cheongju 361-763, Republic of Korea.

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.

KEYWORDS:

Snail; importin β; zinc finger domain

PMID:
23989161
PMCID:
PMC3758161
DOI:
10.1107/S1744309113023038
[Indexed for MEDLINE]
Free PMC Article
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