Publication: Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens
dc.contributor.coauthor | Singh, Nisha | |
dc.contributor.coauthor | Halliday, Amy C. | |
dc.contributor.coauthor | Knight, Matthew | |
dc.contributor.coauthor | Lowe, Edward | |
dc.contributor.coauthor | Churchill, Grant C. | |
dc.contributor.kuauthor | Lack, Nathan Alan | |
dc.contributor.kuprofile | Faculty Member | |
dc.contributor.schoolcollegeinstitute | School of Medicine | |
dc.contributor.yokid | 120842 | |
dc.date.accessioned | 2024-11-09T11:43:35Z | |
dc.date.issued | 2012 | |
dc.description.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 angstrom, respectively. Comparison of MmIMPase 1 and HsIMPase 1 revealed a core r.m.s. deviation of 0.516 angstrom. | |
dc.description.fulltext | YES | |
dc.description.indexedby | WoS | |
dc.description.indexedby | Scopus | |
dc.description.openaccess | YES | |
dc.description.publisherscope | International | |
dc.description.sponsoredbyTubitakEu | N/A | |
dc.description.sponsorship | Biotechnology and Biological Sciences Research Council | |
dc.description.version | Publisher version | |
dc.description.volume | 68 | |
dc.format | ||
dc.identifier.doi | 10.1107/S1744309112035191 | |
dc.identifier.eissn | 2053-230X | |
dc.identifier.embargo | NO | |
dc.identifier.filenameinventoryno | IR00061 | |
dc.identifier.issn | 1744-3091 | |
dc.identifier.link | https://doi.org/10.1107/S1744309112035191 | |
dc.identifier.quartile | Q4 | |
dc.identifier.scopus | 2-s2.0-84867276609 | |
dc.identifier.uri | https://hdl.handle.net/20.500.14288/346 | |
dc.identifier.wos | 309357200002 | |
dc.keywords | Crystallography | |
dc.keywords | Inositol monophosphatase | |
dc.keywords | lithium | |
dc.keywords | bipolar disorder | |
dc.keywords | Myoinositol monophosphatase | |
dc.keywords | Lithium-theraphy | |
dc.keywords | Putative target | |
dc.keywords | Bovine brain | |
dc.keywords | Enzyme | |
dc.language | English | |
dc.publisher | Wiley | |
dc.relation.grantno | BB/I532929/1 | |
dc.relation.uri | http://cdm21054.contentdm.oclc.org/cdm/ref/collection/IR/id/1093 | |
dc.source | Acta Crystallographica Section F, Structural Biology and Crystallization Communications | |
dc.subject | Biochemistry and molecular biology | |
dc.subject | Biophysics | |
dc.title | Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens | |
dc.type | Journal Article | |
dspace.entity.type | Publication | |
local.contributor.authorid | 0000-0001-7399-5844 | |
local.contributor.kuauthor | Lack, Nathan Alan |
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