Biochemical characterization and preliminary study of the domains of human ZBP1 bound X-ray crystallographic to left-handed Z-DNA
Biochemical characterization and preliminary study of the domains of human ZBP1 bound X-ray crystallographic to left-handed Z-DNA
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DOI：
10.1016/j.bbapap.2005.12.012
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发表时间：
2006-02-01
影响因子：
3.2
通讯作者：
Kim, YG
中科院分区：
文献类型：
--
作者：
Ha, SC;Van Quyen, D;Kim, YG
ZBP1参与宿主对细胞应激的反应，包括肿瘤发生和病毒感染。在结构上，它在N端含有两个含有ZA基序的Zα结构域的拷贝。在这里，我们试图用圆二色谱(CD)来表征人类ZBP1中两个Zα结构域--Hzα(ZBP1)和Hz beta(ZBP1)的Z-DNA结合活性。我们的结果表明，HzAlpha(ZBP1)和Hzbeta(ZBP1)都是有活性的Z-DNA结合体，它们的结合活性与先前建立的Za结构域相当。此外，我们还在与Z-DNA的络合物d(TCGCGCG)(2)中结晶了Zβ(ZBP1)。晶体衍射角为1.45埃，属P2(1)2(1)2(1)空间群，晶胞参数a=29.53埃，b=58.25埃，c=88.61埃。这种结构的描绘将提供对不同的ZA基序识别Z-DNA的方式的洞察。(C)2005 Elsevier B.V.保留所有权利。
ZBP1 is involved in host responses against cellular stresses, including tumorigenesis and viral infection. Structurally, it harbors two copies of the Z alpha domain containing the Za motif, at its N terminus. Here, we attempted to characterize the Z-DNA binding activities of two Z alpha domains in the human ZBP1, hZ alpha(ZBP1) and hZ beta(ZBP1), using circular dichroism (CD). Our results indicated that both hZ alpha(ZBP1) and hZ beta(ZBP1) are viable Z-DNA binders, and their binding activities are comparable to those of previously-established Za domains. Additionally, we crystallized hZ beta(ZBP1) in a complex with Z-DNA, d(TCGCGCG)(2). The crystal diffracted to 1.45 angstrom, and belongs to the P2(1)2(1)2(1) space group, with the unit-cell parameters: a=29.53 angstrom, b=58.25 angstrom, and c=88.61 angstrom. The delineation of this structure will provide insight into the manner in which diverse Za motifs recognize Z-DNA. (c) 2005 Elsevier B.V. All rights reserved.