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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

Authors 

S C HaD V QuyenH Y HwangDoo-Byoung OhB A Brown IIS M LeeH J ParkJ H AhnK K KimY G Kim

Publisher 

Elsevier

Issue Date 

2006

Citation 

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol. 1764, no. 2, pp. 320-323

Keywords 

circular dichroismcrystallizationDNA bindingZα motifZ-DNAZBP1DNA binding proteinDNA Zz dna binding protein 1

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.

ISSN 

1570-9639

Link 

http://dx.doi.org/10.1016/j.bbapap.2005.12.012

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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