4as5
From Proteopedia
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| - | [[ | + | ==Structure of mouse inositol monophosphatase 1== |
| + | <StructureSection load='4as5' size='340' side='right' caption='[[4as5]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4as5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AS5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AS5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4as5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4as5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4as5 RCSB], [http://www.ebi.ac.uk/pdbsum/4as5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:23027737</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Inositol Monophosphatase|Inositol Monophosphatase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Inositol-phosphate phosphatase]] | [[Category: Inositol-phosphate phosphatase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Churchill, G C | + | [[Category: Churchill, G C]] |
| - | [[Category: Halliday, A C | + | [[Category: Halliday, A C]] |
| - | [[Category: Knight, M | + | [[Category: Knight, M]] |
| - | [[Category: Lack, N A | + | [[Category: Lack, N A]] |
| - | [[Category: Lowe, E D | + | [[Category: Lowe, E D]] |
| - | [[Category: Singh, N | + | [[Category: Singh, N]] |
[[Category: Bipolar disorder]] | [[Category: Bipolar disorder]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Lithium]] | [[Category: Lithium]] | ||
Revision as of 15:48, 9 December 2014
Structure of mouse inositol monophosphatase 1
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