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dc.contributor.authorBruna, Carola
dc.contributor.authorArriagada, Gloria
dc.contributor.authorLian, Jane B.
dc.contributor.authorStein, Gary S.
dc.contributor.authorBunster, Marta
dc.contributor.authorMartinez-Oyanedel, Jose
dc.contributor.authorMontecino, Martin A.
dc.date2022-08-11T08:08:51.000
dc.date.accessioned2022-08-23T16:09:51Z
dc.date.available2022-08-23T16:09:51Z
dc.date.issued2007-01-18
dc.date.submitted2008-08-11
dc.identifier.citationJ 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.issn0730-2312 (Print)
dc.identifier.doi10.1002/jcb.21231
dc.identifier.pmid17226779
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32797
dc.description.abstractThe 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.isoen_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.urlhttp://dx.doi.org/10.1002/jcb.21231
dc.subjectAbsorptiometry, Photon; Animals; Core Binding Factor Alpha 1 Subunit; Crystallization; Mice; Protein Binding; Protein Structure, Tertiary; Receptors, Calcitriol
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleCrystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor
dc.typeJournal Article
dc.source.journaltitleJournal of cellular biochemistry
dc.source.volume101
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/135
dc.identifier.contextkey573961
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.submissionpathgsbs_sp/135
dc.contributor.departmentDepartment of Cell Biolog
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages785-9


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