کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1179611 | 962785 | 2006 | 4 صفحه PDF | دانلود رایگان |
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 hZαZBP1 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 Å, and belongs to the P212121 space group, with the unit-cell parameters: a = 29.53 Å, b = 58.25 Å, and c = 88.61 Å. The delineation of this structure will provide insight into the manner in which diverse Zα motifs recognize Z-DNA.
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1764, Issue 2, February 2006, Pages 320–323