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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.

Original publication

DOI

10.1107/S1744309112035191

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/10/2012

Volume

68

Pages

1149 - 1152

Keywords

Animals, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Gene Expression, Humans, Inositol Phosphates, Mice, Models, Molecular, Protein Structure, Tertiary