3W5K

Crystal structure of Snail1 and importin beta complex

Summary for 3W5K

• Entry DOI: 10.2210/pdb3w5k/pdb
• Descriptor: Importin subunit beta-1, Zinc finger protein SNAI1, ZINC ION, ... (4 entities in total)
• Functional Keywords: importin beta, nuclear transport factor snail1, transcription repressor, nuclear protein-metal binding protein complex, nuclear protein/metal binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q14974; Nucleus: O95863
• Total number of polymer chains: 2
• Total formula weight: 126641.53

Authors

Choi, S.,Yamashita, E.,Yasuhara, N.,Song, J.,Son, S.Y.,Won, Y.H.,Shin, Y.S.,Sekimoto, T.,Park, I.Y.,Yoneda, Y.,Lee, S.J. (deposition date: 2013-01-30, release date: 2014-03-05, Last modification date: 2024-03-20)

Primary citation

Choi, S.,Yamashita, E.,Yasuhara, N.,Song, J.,Son, S.Y.,Won, Y.H.,Hong, H.R.,Shin, Y.S.,Sekimoto, T.,Park, I.Y.,Yoneda, Y.,Lee, S.J.
Structural basis for the selective nuclear import of the C2H2 zinc-finger protein Snail by importin beta.
Acta Crystallogr.,Sect.D, 70:1050-1060, 2014

PubMed 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 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.

PubMed: 24699649
DOI: 10.1107/S1399004714000972

Experimental method

X-RAY DIFFRACTION (2.6 Å)