Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1α,25 dihydroxy vitamin D3 receptor

Carola Bruna, Gloria Arriagada, Jane B. Lian, Gary S. Stein, Marta Bunster, Jose Martinez-Oyanedel, Martin Montecino

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

5 Citas (Scopus)

Resumen

The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1α,25 dihydroxy vitamin D3, Runx2 may interact with the 1α,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous studies have suggested that the motifs responsible for the VDR-Runx2 interaction are contained within the 230-361 domain of Runx2. In this work, we confirmed by GST-pull down that Runx2l(209-361) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2l(209-361) protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapor-diffusion method and polyethyleneglycol as a precipitant. The crystals were found to diffract to a maximum resolution of 2.7 Å and a complete data set to a 3.3 Å resolution was collected and analyzed. The crystals belong to the tetragonal system, with a space group P4 and unit-cell parameters of a = b = 90.8, and c = 57.2 Å. The presence of a monomer of the recombinant GST-Runx2 l(209-361) in the asymmetric unit gives a VM of 2.7 Å3 Da-1 and a solvent content of 54.8%.

Idioma originalInglés
Páginas (desde-hasta)785-789
Número de páginas5
PublicaciónJournal of Cellular Biochemistry
Volumen101
N.º3
DOI
EstadoPublicada - 1 jun. 2007

Áreas temáticas de ASJC Scopus

  • Bioquímica
  • Biología molecular
  • Biología celular

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