Structural basis for the selective nuclear import of the C2H2 zinc-finger protein Snail by importin β
| Autor: | Yoon Sik Shin, Noriko Yasuhara, Young Han Won, Toshihiro Sekimoto, Hye Rim Hong, Il Yeong Park, Jinsue Song, Eiki Yamashita, Se-Young Son, Soo Jae Lee, Saehae Choi, Yoshihiro Yoneda |
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| Rok vydání: | 2014 |
| Předmět: |
animal structures
Molecular Sequence Data Active Transport Cell Nucleus KLF1 Snail Importin Crystallography X-Ray Cell Line Sequence Analysis Protein Structural Biology Transcription (biology) biology.animal Humans Protein Structure Quaternary chemistry.chemical_classification biology C2H2 Zinc Finger fungi Zinc Fingers General Medicine beta Karyopherins Protein Structure Tertiary Amino acid Cell biology chemistry embryonic structures Snail Family Transcription Factors Nuclear transport Nuclear localization sequence Transcription Factors |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 70:1050-1060 |
| ISSN: | 1399-0047 |
| DOI: | 10.1107/s1399004714000972 |
| Popis: | 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 β directly and as a DNA-binding domain. Here, a 2.5 Å resolution structure of four ZF domains of Snail1 complexed with importin β is presented. The X-ray structure reveals that the four ZFs of Snail1 are required for tight binding to importin β 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 β 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. |
| Databáze: | OpenAIRE |
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