title: Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens.
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.
authors.affiliation: Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, England.
authors.forename: Nisha
authors.initials: N
authors.lastname: Singh
authors.forename: Amy C
authors.initials: AC
authors.lastname: Halliday
authors.forename: Matthew
authors.initials: M
authors.lastname: Knight
authors.forename: Nathan A
authors.initials: NA
authors.lastname: Lack
authors.forename: Edward
authors.initials: E
authors.lastname: Lowe
authors.forename: Grant C
authors.initials: GC
authors.lastname: Churchill
mesh_terms: D000818:Animals; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D006801:Humans; D007295:Inositol Phosphates / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D051379:Mice; D008958:Models, Molecular; D017434:Protein Structure, Tertiary
chemical_list: D007295:Inositol Phosphates