Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4

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dc.contributor.authorJ U Lee-
dc.contributor.authorJ Y Son-
dc.contributor.authorK Y Yoo-
dc.contributor.authorW Shin-
dc.contributor.authorD W Im-
dc.contributor.authorSeung Jun Kim-
dc.contributor.authorS E Ryu-
dc.contributor.authorY S Heo-
dc.date.accessioned2017-04-19T09:56:06Z-
dc.date.available2017-04-19T09:56:06Z-
dc.date.issued2014-
dc.identifier.citationActa Crystallographica. Section F, Structural Biology and Crystallization Communications,70,9,1280,1283ko
dc.identifier.issn1744-3091-
dc.identifier.uri10.1107/S2053230X14017658ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12181-
dc.description.abstractPhosphoinositide 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.publisherInt Union Crystallography-
dc.titleCrystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4-
dc.title.alternativeCrystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4-
dc.typeArticle-
dc.citation.titleActa Crystallographica Section F-Structural Biology-
dc.citation.number9-
dc.citation.endPage1283-
dc.citation.startPage1280-
dc.citation.volume70-
dc.contributor.affiliatedAuthorSeung Jun Kim-
dc.contributor.alternativeName이지운-
dc.contributor.alternativeName손지영-
dc.contributor.alternativeName유기영-
dc.contributor.alternativeName신우리-
dc.contributor.alternativeName임동원-
dc.contributor.alternativeName김승준-
dc.contributor.alternativeName류성언-
dc.contributor.alternativeName허용석-
dc.identifier.bibliographicCitationActa Crystallographica Section F-Structural Biology, vol. 70, no. 9, pp. 1280-1283-
dc.identifier.doi10.1107/S2053230X14017658-
dc.subject.keywordMTMR4-
dc.subject.keywordmyotubularin-related proteins-
dc.subject.keywordPH-GRAM domain-
dc.subject.keywordphosphatase-
dc.subject.keywordphosphoinositide-
dc.subject.localMTMR4-
dc.subject.localmyotubularin-related proteins-
dc.subject.localPH-GRAM domain-
dc.subject.localPhosphatases-
dc.subject.localphosphatase-
dc.subject.localPhosphatase-
dc.subject.localPhosphoinositide-
dc.subject.localphosphoinositide-
dc.description.journalClassY-
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