Crystallographic analysis of an anticancer target enzyme at high resolution
| Project/Area Number |
18K06600
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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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| Review Section |
Basic Section 47020:Pharmaceutical analytical chemistry and physicochemistry-related
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| Research Institution | Kumamoto University |
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Principal Investigator |
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2020: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2019: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2018: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 構造生物学 / X線結晶構造解析 / 中性子結晶構造解析 |
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| Outline of Final Research Achievements |
In this research, we investigated mechanisms of an enzymatic reaction and inhibitor binding of an oxidized nucleotide hydrolase. We carried out the crystallization under microgravity and determined the high-resolution crystal structure. The structure revealed the protonation state in the active site with higher accuracy and precision. In addition, we obtained structural insights into the substrate specificity of the hydrolase by experiments of X-ray crystallography, activity measurement, and substrate binding.
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| Academic Significance and Societal Importance of the Research Achievements |
酵素などのタンパク質の機能を原子レベルで理解するには、水素原子までをも明らかにする精密構造解析が必要不可欠である。本研究では、酸化ヌクレオチド加水分解酵素の精密構造解析を行うことで、酵素反応機構、阻害剤結合において重要な活性部位の水素原子を含めた構造情報を得た。
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Report
(4 results)
Research Products
(14 results)
