Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor
dc.contributor.author | Bruna, Carola | |
dc.contributor.author | Arriagada, Gloria | |
dc.contributor.author | Lian, Jane B. | |
dc.contributor.author | Stein, Gary S. | |
dc.contributor.author | Bunster, Marta | |
dc.contributor.author | Martinez-Oyanedel, Jose | |
dc.contributor.author | Montecino, Martin A. | |
dc.date | 2022-08-11T08:08:51.000 | |
dc.date.accessioned | 2022-08-23T16:09:51Z | |
dc.date.available | 2022-08-23T16:09:51Z | |
dc.date.issued | 2007-01-18 | |
dc.date.submitted | 2008-08-11 | |
dc.identifier.citation | J Cell Biochem. 2007 Jun 1;101(3):785-9. <a href="http://dx.doi.org/10.1002/jcb.21231">Link to article on publisher's site</a> | |
dc.identifier.issn | 0730-2312 (Print) | |
dc.identifier.doi | 10.1002/jcb.21231 | |
dc.identifier.pmid | 17226779 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/32797 | |
dc.description.abstract | The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,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 Runx2(I(209-361)) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2(I(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 A and a complete data set to a 3.3 A 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 A. The presence of a monomer of the recombinant GST-Runx2(I(209-361)) in the asymmetric unit gives a V(M) of 2.7 A(3) Da(-1) and a solvent content of 54.8%. | |
dc.language.iso | en_US | |
dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17226779&dopt=Abstract ">Link to article in PubMed</a> | |
dc.relation.url | http://dx.doi.org/10.1002/jcb.21231 | |
dc.subject | Absorptiometry, Photon; Animals; Core Binding Factor Alpha 1 Subunit; Crystallization; Mice; Protein Binding; Protein Structure, Tertiary; Receptors, Calcitriol | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor | |
dc.type | Journal Article | |
dc.source.journaltitle | Journal of cellular biochemistry | |
dc.source.volume | 101 | |
dc.source.issue | 3 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/135 | |
dc.identifier.contextkey | 573961 | |
html.description.abstract | <p>The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,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 Runx2(I(209-361)) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2(I(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 A and a complete data set to a 3.3 A 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 A. The presence of a monomer of the recombinant GST-Runx2(I(209-361)) in the asymmetric unit gives a V(M) of 2.7 A(3) Da(-1) and a solvent content of 54.8%.</p> | |
dc.identifier.submissionpath | gsbs_sp/135 | |
dc.contributor.department | Department of Cell Biolog | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 785-9 |