Elucidation of the oligomerization mechanism of pore forming protein
| Project/Area Number |
23780107
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
GODA Shuichiro 長崎大学, 大学院・工学研究科, 准教授 (00346587)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | タンパク質工学 / 蛋白質 / タンパク質 / 生体分子 / 糖鎖 |
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| Research Abstract |
Pore forming proteins form oligomer on the surface of the cell. Then, they form an ion permiable pore to disrupt the cells. In this reseach, structural changes in oligomerization and oligomeric stucture of the pore forming proteins were measured by small-angle X-ray scattering (SAXS) and crystal X-ray diffraction. A hemolytic lectin from marine invertebrate Cucumaria echinata (CEL-III) forms heptamer at first then three heptamers form 21-mer and 21-mer dissociated to heptamer in the presence of detergent by the results of SAXS measurements. CEL-III oligomer was crystallized and X-ray diffraction data were collected. Crystals diffracted X-rays to 3.3 and 4.2 A resolution using synchrotron radiation.
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Report
(3 results)
Research Products
(39 results)
