Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4
DC Field | Value | Language |
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dc.contributor.author | Lee, Jee Un | - |
dc.contributor.author | Son, Ji Young | - |
dc.contributor.author | Yoo, Ki-Young | - |
dc.contributor.author | Shin, Woori | - |
dc.contributor.author | Im, Dong-Won | - |
dc.contributor.author | Kim, Seung Jun | - |
dc.contributor.author | Ryu, Seong Eon | - |
dc.contributor.author | Heo, Yong-Seok | - |
dc.date.accessioned | 2022-07-16T03:08:25Z | - |
dc.date.available | 2022-07-16T03:08:25Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2014-09 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/159209 | - |
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 angstrom resolution at a synchrotron beamline and belonged to either space group P6(1) or P6(5), with unit-cell parameters a = b = 109.10, c = 238.97 angstrom. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | INT UNION CRYSTALLOGRAPHY | - |
dc.title | Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4 | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Ryu, Seong Eon | - |
dc.identifier.doi | 10.1107/S2053230X14017658 | - |
dc.identifier.scopusid | 2-s2.0-84907031823 | - |
dc.identifier.wosid | 000341818600033 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.1280 - 1283 | - |
dc.relation.isPartOf | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | - |
dc.citation.volume | 70 | - |
dc.citation.startPage | 1280 | - |
dc.citation.endPage | 1283 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Crystallography | - |
dc.subject.keywordPlus | MYOTUBULARIN-RELATED PROTEIN-2 | - |
dc.subject.keywordPlus | PHOSPHATASES | - |
dc.subject.keywordPlus | MYOPATHY | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | PHOSPHOINOSITIDES | - |
dc.subject.keywordPlus | ENDOSOMES | - |
dc.subject.keywordPlus | MUTATIONS | - |
dc.subject.keywordAuthor | MTMR4 | - |
dc.subject.keywordAuthor | myotubularin-related proteins | - |
dc.subject.keywordAuthor | PH-GRAM domain | - |
dc.subject.keywordAuthor | phosphatase | - |
dc.subject.keywordAuthor | phosphoinositide | - |
dc.identifier.url | http://scripts.iucr.org/cgi-bin/paper?S2053230X14017658 | - |
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