Crystallization and preliminary X-ray diffraction analysis of human importin ß-Snail zinc finger domain complex.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 69(Pt 9): 1049-51, 2013 Sep.
Article
in En
| MEDLINE
| ID: mdl-23989161
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 ß through direct binding with its four zinc finger domain. The complex between importin ß 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 = 72.0â
Å, ß = 100.9° and diffracted to 2.5â
Å resolution.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Transcription Factors
/
Beta Karyopherins
Limits:
Humans
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2013
Document type:
Article