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|Title:||Cloning, purification and preliminary X-ray data analysis of the human ID2 homodimer|
inhibitor of DNA binding
|Source:||Wong, M.V., Palasingam, P., Kolatkar, P.R. (2012-11). Cloning, purification and preliminary X-ray data analysis of the human ID2 homodimer. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 68 (11) : 1354-1358. ScholarBank@NUS Repository. https://doi.org/10.1107/S174430911203895X|
|Abstract:||The ID proteins are named for their role as inhibitors of DNA binding and differentiation. They contain a helix-loop-helix (HLH) domain but lack a basic DNA-binding domain. In complex with basic HLH (bHLH) transcription factors, gene expression is regulated by DNA-binding inactivation. Although the HLH domain is highly conserved and shares a similar topology, the IDs preferentially bind class I bHLH-group members such as E47 (TCF3) but not the class III bHLH member Myc. A structure of an ID protein could potentially shed light on its mechanism. Owing to their short half-lives in vivo and reported in vitro instability, this paper describes the strategies that went into expressing sufficient soluble and stable ID2 to finally obtain diffraction-quality crystals. A 2.1 Å resolution data set was collected from a crystal belonging to space group P3121 with unit-cell parameters a = b = 51.622, c = 111.474 Å, = Β = 90, = 120° that was obtained by hanging-drop vapour diffusion in a precipitant solution consisting of 0.1 M MES pH 6.5, 2.0 M potassium acetate. The solvent content was consistent with the presence of one or two molecules in the asymmetric unit. © 2012 International Union of Crystallography All rights reserved.|
|Source Title:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Appears in Collections:||Staff Publications|
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