4AS4

Structure of human inositol monophosphatase 1

Summary for 4AS4

• Entry DOI: 10.2210/pdb4as4/pdb
• Related: 1AWB 1IMA 1IMB 1IMC 1IMD 1IME 1IMF 2HHM 4AS5
• Descriptor: INOSITOL MONOPHOSPHATASE 1, PHOSPHATE ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase, lithium, bipolar disorder
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P29218
• Total number of polymer chains: 2
• Total formula weight: 61419.99

Authors

Singh, N.,Knight, M.,Halliday, A.C.,Lack, N.A.,Lowe, E.D.,Churchill, G.C. (deposition date: 2012-04-27, release date: 2012-10-10, Last modification date: 2024-11-13)

Primary citation

Singh, N.,Halliday, A.C.,Knight, M.,Lack, N.A.,Lowe, E.D.,Churchill, G.C.
Cloning, Expression, Purification, Crystallization and X-Ray Analysis of Inositol Monophosphatase from Mus Musculus and Homo Sapiens.
Acta Crystallogr.,Sect.F, 68:1149-, 2012

PubMed 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.

PubMed: 23027737
DOI: 10.1107/S1744309112035191

Experimental method

X-RAY DIFFRACTION (1.7 Å)