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

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 ? through direct binding with its four zinc finger domain. The complex between importin ? 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, ? = 100.9° and diffracted to 2.5?Å resolution.

SUBMITTER: Choi S

PROVIDER: S-EPMC3758161 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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

Choi Saehae S Song Jinsue J Son Se-Young SY Park Il Yeong IY Yamashita Eiki E Lee Soo Jae SJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20130823 Pt 9

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 separ ...[more]

PMID: 23989161

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