4as5 | pdb_00004as5

Structure of mouse inositol monophosphatase 1

spinqualitylabelsall models 4as5, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4as5 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, GOL, IOD, MG, PO4 Activity: Inositol-phosphate phosphatase, with EC number 3.1.3.25 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 A, respectively. Comparison of MmIMPase 1 and HsIMPase 1 revealed a core r.m.s. deviation of 0.516 A. Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens.,Singh N, Halliday AC, Knight M, Lack NA, Lowe E, Churchill GC Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1149-52., doi: 10.1107/S1744309112035191. Epub 2012 Sep 22. PMID:23027737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Inositol Monophosphatase

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