2. Academic Validation
  3. 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

  • Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1149-52. doi: 10.1107/S1744309112035191.
Nisha Singh 1,  Amy C Halliday,  Matthew Knight,  Nathan A Lack,  Edward Lowe,  Grant C Churchill
Affiliations

Affiliation

  • 1 Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, England.
PMID: 23027737 DOI: 10.1107/S1744309112035191
Abstract

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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