2016 Fiscal Year Final Research Report
Investigation of molecular mechanism of transphosphorylation by a phosphatidylinositol kinase
Project/Area Number |
15H06855
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Physical pharmacy
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Research Institution | High Energy Accelerator Research Organization |
Principal Investigator |
SATO Tomomi 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 博士研究員 (20759211)
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Research Collaborator |
TAKEUCHI Ko 産業技術総合研究所, 創薬分子プロファイリングセンター, 主任研究員
SASAKI Atsuo University of Cincinnati, Associate Professor
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Project Period (FY) |
2015-08-28 – 2017-03-31
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Keywords | 構造生物学 / キナーゼ / 相互作用解析 / イノシトールリン脂質 / 結晶化 / PI5P4K / リン酸化反応機構 / X線結晶構造解析 |
Outline of Final Research Achievements |
In this research project, I performed following three experiments in order to elucidate catalytic mechanism of phosphorylation by an inositol phospholipid kinase, PI5P4K beta. 1) Interaction analysis between PI5P4K beta and lipid/nucleotide by SPR, 2) X-ray crystallographic structural analysis in complex with inhibitors, 3) Crystallization of PI5P4K alpha/gamma. From the results of the SPR analysis, I elucidated that the interaction between background lipid and PI5P4K beta is relatively strong (micro molar order) while the intersection between substrate (PI5P) and PI5P4K beta is predicted to be weak. I also succeeded in observation of electron density of 3 inhibitors and crystallization of PI5P4K alpha.
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Free Research Field |
構造生物学
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