• Login
    View Item 
    •   Home
    • UMass Chan Student Research and Publications
    • Morningside Graduate School of Biomedical Sciences
    • Morningside Graduate School of Biomedical Sciences Scholarly Publications
    • View Item
    •   Home
    • UMass Chan Student Research and Publications
    • Morningside Graduate School of Biomedical Sciences
    • Morningside Graduate School of Biomedical Sciences Scholarly Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of eScholarship@UMassChanCommunitiesPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsThis CollectionPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywords

    My Account

    LoginRegister

    Help

    AboutSubmission GuidelinesData Deposit PolicySearchingAccessibilityTerms of UseWebsite Migration FAQ

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

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

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Bruna, Carola
    Arriagada, Gloria
    Lian, Jane B.
    Stein, Gary S.
    Bunster, Marta
    Martinez-Oyanedel, Jose
    Montecino, Martin A.
    UMass Chan Affiliations
    Department of Cell Biolog
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2007-01-18
    Keywords
    Absorptiometry, Photon; Animals; Core Binding Factor Alpha 1 Subunit; Crystallization; Mice; Protein Binding; Protein Structure, Tertiary; Receptors, Calcitriol
    Life Sciences
    Medicine and Health Sciences
    
    Metadata
    Show full item record
    Link to Full Text
    http://dx.doi.org/10.1002/jcb.21231
    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%.
    Source
    J Cell Biochem. 2007 Jun 1;101(3):785-9. Link to article on publisher's site
    DOI
    10.1002/jcb.21231
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32797
    PubMed ID
    17226779
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1002/jcb.21231
    Scopus Count
    Collections
    Morningside Graduate School of Biomedical Sciences Scholarly Publications

    entitlement

    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Lamar Soutter Library, UMass Chan Medical School | 55 Lake Avenue North | Worcester, MA 01655 USA
    Quick Guide | escholarship@umassmed.edu
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.