Structural biological studies on the sialic acid-binding mechanism of R-type lectin mutant
| Project/Area Number |
24580500
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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 |
Applied molecular and cellular biology
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| Research Institution | National Agriculture and Food Research Organization |
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Principal Investigator |
HEMMI Hikaru 独立行政法人農業・食品産業技術総合研究機構, 食品総合研究所食品分析研究領域, 上席研究員 (70353993)
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| Co-Investigator(Kenkyū-buntansha) |
KUNO Atsushi 独立行政法人産業技術総合研究所, 糖鎖創薬技術研究センター, 上級主任研究員 (50302287)
HIRABAYASHI Jun 独立行政法人産業技術総合研究所, 幹細胞工学研究センター, 首席研究員 (40156691)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 蛋白質 / 糖鎖 / NMR / レクチン / 糖認識ドメイン |
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| Outline of Final Research Achievements |
We performed the nuclear magnetic resonance analysis of the sialic acid-binding mechanism of the novel sialic acid-binding lectin (SRC) produced from the C-terminal domain of the novel R-type lectin from the earthworm (EW29Ch) by natural evolution-mimicry. The results showed that in the 6’-sialyllactose-bound state SRC has two conformations different from both the conformation in the sugar-free state and that in the lactose-bound state. Further, the internal motion of the loop region in subdomain γ of SRC remarkably changed from that of the corresponding region in subdomain γ of the wild type lectin EW29Ch, indicating that the internal motion change is important in the sialic acid-binding mechanism of SRC.
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Report
(4 results)
Research Products
(8 results)
