Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the human TLE1 Q domain
Human transducin-like enhancer of split 1 (TLE1) plays crucial roles in a number of developmental processes and is involved in pathogenesis of malignancy tumors. The N-terminal glutamine-rich domain (Q domain) of TLE1 mediates its tetramerization and interactions with different DNA-binding transcrip...
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Veröffentlicht in: | Acta biochimica et biophysica Sinica 2011-02, Vol.43 (2), p.149-153 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Human transducin-like enhancer of split 1 (TLE1) plays crucial roles in a number of developmental processes and is involved in pathogenesis of malignancy tumors. The N-terminal glutamine-rich domain (Q domain) of TLE1 mediates its tetramerization and interactions with different DNA-binding transcription factors to regulate Notch and Wnt signaling pathways. To better understand the molecular mechanism of TLE1's functions in these pathways, we cloned, purified, and crystallized the TLE1 Q domain (TLE1-Q). The crystals belong to space group C2221, with the complete diffraction data of the native and Se-Met TLE1-Q collected to 3.5 and 4.1A resol- utions, respectively. The phasing-solving and model build- ing are in progress. |
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ISSN: | 1672-9145 1745-7270 |
DOI: | 10.1093/abbs/gmq116 |