Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens.

Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens.
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小家鼠和智人肌醇单磷酸酶的克隆、表达、纯化、结晶和 X 射线分析。

DOI:
10.1107/s1744309112035191
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发表时间:
2012
期刊:
Acta crystallographica. Section F, Structural biology and crystallization communications
影响因子:
--
通讯作者:
Singh N
Singh N
中科院分区:
--
文献类型:
--
作者:
Singh N

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肌醇单磷酸酶(IMPase)催化单磷酸肌醇水解为肌醇,在磷脂酰肌醇(PI)信号通路中起关键作用。锂是治疗双相情感障碍的首选药物,在治疗相关的血浆浓度下抑制IMPase。将小鼠IMPase 1 (MmIMPase 1)和人IMPase 1 (HsIMPase 1)克隆到pRSET5a中,在大肠杆菌中表达,采用坐滴法纯化结晶。这些结构分别在2.4和1.7分辨率下进行求解Å。MmIMPase 1和HsIMPase 1的比较显示核心均方根偏差为0.516 Å。
Inositol monophosphatase (IMPase) catalyses the hydrolysis of inositol monophosphate to inositol and is crucial in the phosphatidylinositol (PI) signalling pathway. Lithium, which is the drug of choice for bipolar disorder, inhibits IMPase at therapeutically relevant plasma concentrations. Both mouse IMPase 1 (MmIMPase 1) and human IMPase 1 (HsIMPase 1) were cloned into pRSET5a, expressed in Escherichia coli, purified and crystallized using the sitting-drop method. The structures were solved at resolutions of 2.4 and 1.7 Å, respectively. Comparison of MmIMPase 1 and HsIMPase 1 revealed a core r.m.s. deviation of 0.516 Å.
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