Elucidation of the dynamic structural change of hemolytic lectin in pore forming
| Project/Area Number |
16K07695
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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 biochemistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2018: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 溶血性レクチン / 孔形成毒素 / Ｘ線小角散乱 / レクチン / 溶血性 / 蛋白質 / 糖鎖 |
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| Outline of Final Research Achievements |
Elucidation of the pore forming mechanism of hemolytic lectin CEL-III was done. Tertiary structure of the pore forming CEL-III showed that the pore region is consist of stem, wrapping and bundle region. Deletion mutants that lost stem region, stem and wrapping region were made and quaternary structures were analyzed by small-angle x-ray scattering. The results showed that the stem deleted mutant formed heptameric form and stem and wrapping region deleted mutant exist as monomer. This result indicates that the oligomerization is not depend on the stem region, and wrapping region affect the oligomerization. This suggests that the CEL-III forms heptamer at first on the surface of the cell membrane, and then forms pore in the cell membrane.
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| Academic Significance and Societal Importance of the Research Achievements |
膜孔形成毒素はタンパク質を原因とする疾病を引き起こし、タンパク質が四次構造変化、すなわち多量体化するとともに立体構造が変化して孔を形成することによって起こる。このことはタンパク質が一つの安定した構造で存在するのではなく環境に応じて立体構造を変化させる好例であり、立体構造形成の研究の観点からも注目されている。本研究は、その多量体化機構の解明につながるものであり、多量体化の後に孔形成が行われる機序を明らかとしたことは四次構造変化を含む立体構造形成に与える学術的意義が大きい。これらタンパク質の立体構造変化による疾病は他にも広く知られており、その機構の解明は社会的意義も大きい。
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Report
(4 results)
Research Products
(19 results)
