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...
| Główni autorzy: | , , , , , |
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| Format: | Journal article |
| Język: | English |
| Wydane: |
2012
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| _version_ | 1826268568706088960 |
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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. |
| first_indexed | 2024-03-06T21:11:41Z |
| format | Journal article |
| id | oxford-uuid:3e6665b3-84b4-401d-8863-ac0b846daa46 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:11:41Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:3e6665b3-84b4-401d-8863-ac0b846daa462022-03-26T14:25:13ZCloning, expression, purification, crystallization and X-ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3e6665b3-84b4-401d-8863-ac0b846daa46EnglishSymplectic 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. |
| 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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