Biochemical characterization and preliminary X-ray crystallographic study of the domains of human ZBP1 bound to left-handed Z-DNA

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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
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