2bji
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(New page: 200px<br /> <applet load="2bji" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bji, resolution 1.24Å" /> '''HIGH RESOLUTION STR...)
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Revision as of 18:13, 29 October 2007
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HIGH RESOLUTION STRUCTURE OF MYO-INOSITOL MONOPHOSPHATASE, THE TARGET OF LITHIUM THERAPY
Overview
Inositol monophosphatase is a key enzyme of the phosphatidylinositol, signalling pathway and the putative target of the mood-stabilizing drug, lithium. The crystal structure of bovine inositol monophosphatase has been, determined at 1.4 A resolution in complex with the physiological magnesium, ion ligands. Three magnesium ions are octahedrally coordinated at the, active site of each of the two subunits of the inositol monophosphatase, dimer and a detailed three-metal mechanism is proposed. Ligands to the, three metals include the side chains of Glu70, Asp90, Asp93 and Asp220, the backbone carbonyl group of Ile92 and several solvent molecules, including the proposed nucleophilic water molecule (W1) ligated by both, Mg-1 and Mg-3. Modelling of the phosphate moiety of inositol monophosphate, ... [(full description)]
About this Structure
2BJI is a [Single protein] structure of sequence from [Bos taurus] with MG as [ligand]. Active as [[1]], with EC number [3.1.3.25]. Full crystallographic information is available from [OCA].
Reference
High-resolution structure of myo-inositol monophosphatase, the putative target of lithium therapy., Gill R, Mohammed F, Badyal R, Coates L, Erskine P, Thompson D, Cooper J, Gore M, Wood S, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):545-55. Epub 2005, Apr 20. PMID:15858264
Page seeded by OCA on Mon Oct 29 20:18:15 2007
Categories: Bos taurus | Single protein | Badyal, R. | Coates, L. | Cooper, J. | Erskine, P. | Gill, R. | Gore, M. | Mohammed, F. | Thompson, D. | Wood, S. | MG | Aspartic proteinase mechanism | Aspartyl protease | Hydrolase | Succinimide | Zymogen