DC Field | Value | Language |
---|---|---|
dc.contributor.author | J U Lee | - |
dc.contributor.author | J Y Son | - |
dc.contributor.author | K Y Yoo | - |
dc.contributor.author | W Shin | - |
dc.contributor.author | D W Im | - |
dc.contributor.author | Seung Jun Kim | - |
dc.contributor.author | S E Ryu | - |
dc.contributor.author | Y S Heo | - |
dc.date.accessioned | 2017-04-19T09:56:06Z | - |
dc.date.available | 2017-04-19T09:56:06Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Acta Crystallographica. Section F, Structural Biology and Crystallization Communications,70,9,1280,1283 | ko |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | 10.1107/S2053230X14017658 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/12181 | - |
dc.description.abstract | Phosphoinositide lipid molecules play critical roles in intracellular signalling pathways and are regulated by phospholipases, lipid kinases and phosphatases. In particular, phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate are related to endosomal trafficking events through the recruitment of effector proteins and are involved in the degradation step of autophagy. Myotubularin-related proteins (MTMRs) are a large family of phosphatases that catalyze the dephosphorylation of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at the D3 position, thereby regulating cellular phosphoinositide levels. In this study, the PH-GRAM domain of human MTMR4 was cloned, overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method. The crystals diffracted to 3.20 A resolution at a synchrotron beamline and belonged to either space group P61 or P65, with unit-cell parameters a = b = 109.10, c = 238.97 A. | - |
dc.publisher | Int Union Crystallography | - |
dc.title | Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4 | - |
dc.title.alternative | Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4 | - |
dc.type | Article | - |
dc.citation.title | Acta Crystallographica Section F-Structural Biology | - |
dc.citation.number | 9 | - |
dc.citation.endPage | 1283 | - |
dc.citation.startPage | 1280 | - |
dc.citation.volume | 70 | - |
dc.contributor.affiliatedAuthor | Seung Jun Kim | - |
dc.contributor.alternativeName | 이지운 | - |
dc.contributor.alternativeName | 손지영 | - |
dc.contributor.alternativeName | 유기영 | - |
dc.contributor.alternativeName | 신우리 | - |
dc.contributor.alternativeName | 임동원 | - |
dc.contributor.alternativeName | 김승준 | - |
dc.contributor.alternativeName | 류성언 | - |
dc.contributor.alternativeName | 허용석 | - |
dc.identifier.bibliographicCitation | Acta Crystallographica Section F-Structural Biology, vol. 70, no. 9, pp. 1280-1283 | - |
dc.identifier.doi | 10.1107/S2053230X14017658 | - |
dc.subject.keyword | MTMR4 | - |
dc.subject.keyword | myotubularin-related proteins | - |
dc.subject.keyword | PH-GRAM domain | - |
dc.subject.keyword | phosphatase | - |
dc.subject.keyword | phosphoinositide | - |
dc.subject.local | MTMR4 | - |
dc.subject.local | myotubularin-related proteins | - |
dc.subject.local | PH-GRAM domain | - |
dc.subject.local | Phosphatases | - |
dc.subject.local | phosphatase | - |
dc.subject.local | Phosphatase | - |
dc.subject.local | Phosphoinositide | - |
dc.subject.local | phosphoinositide | - |
dc.description.journalClass | Y | - |
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