| Project/Area Number |
15K07935
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Nagoya City University |
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Principal Investigator |
Yagi Hirokazu 名古屋市立大学, 大学院薬学研究科, 講師 (70565423)
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| Co-Investigator(Renkei-kenkyūsha) |
KATO Koichi 名古屋市立大学, 大学院薬学研究科, 教授 (20211849)
SUGIYAMA Masaaki 京都大学, 複合原子力科学研究所, 教授 (10253395)
SATOH Tadashi 名古屋市立大学, 大学院薬学研究科, 准教授 (80532100)
YAMAGUCHI Takumi 北陸先端科学技術大学院大学, マテリアルサイエンス系, 准教授 (60522430)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | LARGE / K4CP / 糖転移酵素 / 高速AFM / 糖鎖伸長 / バイファンクショナルな糖転移酵素 / Ｘ線小角散乱 / 非変性質量分析 / 筋ジストロフィー |
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| Outline of Final Research Achievements |
LARGE (Like-acetylglucosaminyltransferase) is the causative gene product for congenital muscular dystrophy which possesses two catalytic domains with homology to members of glycosyltransferases to form a repeat sequence of xylose and glucuronic acid residues. In this study, we have performed a molecular dynamics study to characterize the mechanism that the enzymes composed of these two catalytic domains catalyze the elongation reactions of sugar chains. As a result, the enzymes exhibited dynamic motions involving domain-domain association and dissociation during the reaction, indicating that orientation between the two domains would contribute to the elongation efficiency to exchange the substrate sugar chain.
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