Crystallization and preliminary X-ray crystallographic analysis of the human CKIP-1 pleckstrin homology domain.
Crystallization and preliminary X-ray crystallographic analysis of the human CKIP-1 pleckstrin homology domain.
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DOI：
10.1107/s1744309113003382
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发表时间：
2013-03
期刊：
影响因子：
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通讯作者：
Ping Li;Yuli Xu;Xin Li;M. Bartlam
中科院分区：
文献类型：
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作者：
Ping Li;Yuli Xu;Xin Li;M. Bartlam
酪蛋白激酶2相互作用蛋白-1（CKIP-1）参与许多细胞功能，包括细胞凋亡、信号传导途径、细胞生长、细胞骨架和骨形成。其N-末端普列克底物蛋白同源（PH）结构域被认为在膜定位中起重要作用，并控制CKIP-1在质膜和细胞核之间的穿梭。在这项研究中，人CKIP-1 PH结构域被纯化，但遇到了核酸污染的问题。纯化并成功结晶了设计用于消除核酸结合的S84 D/S86 D/S88 D三重突变体。单晶衍射分辨率为1.7 μ m，空间群为P4 <$2 <$2，晶胞参数a=53.0，B=53.0，c=113.8 μ m，α=β=γ=90.0°。
The casein kinase 2 interacting protein-1 (CKIP-1) is involved in many cellular functions, including apoptosis, signalling pathways, cell growth, cytoskeleton and bone formation. Its N-terminal pleckstrin homology (PH) domain is thought to play an important role in membrane localization and controls shuttling of CKIP-1 between the plasma membrane and nucleus. In this study, the human CKIP-1 PH domain was purified but problems were encountered with nucleic acid contamination. An S84D/S86D/S88D triple mutant designed to abolish nucleic acid binding was purified and successfully crystallized. Single crystals diffracted to 1.7 Å resolution and belonged to space group P4₃2₁2 with unit-cell parameters a=53.0, b=53.0, c=113.8 Å, α=β=γ=90.0°.