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- Title
- Biochemical characterization and preliminary X-ray crystallographic study of the domains of human ZBP1 bound to left-handed Z-DNA
- Author(s)
- S C Ha; D V Quyen; H Y Hwang; Doo-Byoung Oh; B A Brown II; S M Lee; H J Park; J H Ahn; K K Kim; Y G Kim
- Bibliographic Citation
- Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1764, no. 2, pp. 320-323
- Publication Year
- 2006
- Abstract
- ZBP1 is involved in host responses against cellular stresses, including tumorigenesis and viral infection. Structurally, it harbors two copies of the Zα domain containing the Zα motif, at its N terminus. Here, we attempted to characterize the Z-DNA binding activities of two Zα domains in the human ZBP1, hZαZBP1 and hZβZBP1, using circular dichroism (CD). Our results indicated that both hZα ZBP1 and hZβZBP1 are viable Z-DNA binders, and their binding activities are comparable to those of previously-established Zα domains. Additionally, we crystallized hZβZBP1 in a complex with Z-DNA, d(TCGCGCG)2. The crystal diffracted to 1.45 ?, and belongs to the P212121 space group, with the unit-cell parameters: a = 29.53 ?, b = 58.25 ?, and c = 88.61 ?. The delineation of this structure will provide insight into the manner in which diverse Zα motifs recognize Z-DNA.
- Keyword
- Circular dichroismCrystallizationDNA bindingZα motifZ-DNAZBP1
- ISSN
- 1570-9639
- Publisher
- Elsevier
- DOI
- http://dx.doi.org/10.1016/j.bbapap.2005.12.012
- Type
- Article
- Appears in Collections:
- Aging Convergence Research Center > 1. Journal Articles
- Files in This Item:
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