Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens
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 mous...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2012
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| _version_ | 1826257155580231680 |
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| author | Singh, N Halliday, A Knight, M Lack, N Lowe, E Churchill, G |
| author_facet | Singh, N Halliday, A Knight, M Lack, N Lowe, E Churchill, G |
| author_sort | Singh, N |
| collection | OXFORD |
| description | 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. © 2012 International Union of Crystallography. |
| first_indexed | 2024-03-06T18:13:38Z |
| format | Journal article |
| id | oxford-uuid:03ddbb38-f42a-4044-bd89-2bf561875853 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:13:38Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:03ddbb38-f42a-4044-bd89-2bf5618758532022-03-26T08:48:35ZCloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiensJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:03ddbb38-f42a-4044-bd89-2bf561875853EnglishSymplectic Elements at Oxford2012Singh, NHalliday, AKnight, MLack, NLowe, EChurchill, GInositol 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. © 2012 International Union of Crystallography. |
| spellingShingle | Singh, N Halliday, A Knight, M Lack, N Lowe, E Churchill, G Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens |
| title | Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens |
| title_full | Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens |
| title_fullStr | Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens |
| title_full_unstemmed | Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens |
| title_short | Cloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens |
| title_sort | cloning expression purification crystallization and x ray analysis of inositol monophosphatase from mus musculus and homo sapiens |
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