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Acta Crystallogr D Biol Crystallogr ; 70(Pt 4): 1050-60, 2014 Apr.
Article in English | MEDLINE | ID: mdl-24699649

ABSTRACT

Snail contributes to the epithelial-mesenchymal transition by suppressing E-cadherin in transcription processes. The Snail C2H2-type zinc-finger (ZF) domain functions both as a nuclear localization signal which binds to importin ß directly and as a DNA-binding domain. Here, a 2.5 Šresolution structure of four ZF domains of Snail1 complexed with importin ß is presented. The X-ray structure reveals that the four ZFs of Snail1 are required for tight binding to importin ß in the nuclear import of Snail1. The shape of the ZFs in the X-ray structure is reminiscent of a round snail, where ZF1 represents the head, ZF2-ZF4 the shell, showing a novel interaction mode, and the five C-terminal residues the tail. Although there are many kinds of C2H2-type ZFs which have the same fold as Snail, nuclear import by direct recognition of importin ß is observed in a limited number of C2H2-type ZF proteins such as Snail, Wt1, KLF1 and KLF8, which have the common feature of terminating in ZF domains with a short tail of amino acids.


Subject(s)
Transcription Factors/chemistry , Zinc Fingers , beta Karyopherins/chemistry , Active Transport, Cell Nucleus , Cell Line , Crystallography, X-Ray , Humans , Molecular Sequence Data , Protein Structure, Quaternary , Protein Structure, Tertiary , Sequence Analysis, Protein , Snail Family Transcription Factors , Transcription Factors/metabolism , beta Karyopherins/metabolism
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